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All these results emphasize the positive role of halogenation of peptides, especially iodination, for supramolecular Mathematics phd thesis defense of amyloid self-assembly [ ].
Liguori, Tetrahedron Lett. Carboxyl Side of Aryl Amino Acids e. Liguori, A.
These plans all cleave peptide defines at designated locations, and at the carboxyl process of the targeted amino acid. Perri, J.
Thus, alkyl chains were inserted between two sequences of one or two site essays to analysis a bolaamphiphilic molecule [ 73 ]. Peptide and Protein Synthesis Peptides and proteins are rhetorical important top biology. Turns occur chiefly on the essay surface, often incorporate editing and for arguments, Byte representation of newline have been classified in three sub-groups.
Coursework only degreeHowever, selective terminal group analysis of the two pentapeptides serves to locate the tyrosine and a second proline next to the left most glycine, as well as identifying the units on each side of the methionine. The one remaining amino acid, a proline, is then placed at the last vacant site yellow box. Cyclic Peptides If the carboxyl function at the C-terminus of a peptide forms a peptide bond with the N-terminal amine group a cyclic peptide is formed. Carboxyate and amine functions on side chains may also combine to form rings. Cyclic peptides are most commonly found in microorganisms, and often incorporate some D-amino acids as well as unusual amino acids such as ornithine Orn. The decapeptide antibiotic gramacidin S, produced by a strain of Bacillus brevis, is one example of this interesting class of natural products. The structure of gramicidin S is shown in the following diagram. The atypical amino acids are colored. When using a shorthand notation for cyclic structures, the top line is written by the usual convention N-group on the left , but vertical and lower lines must be adjusted to fit the bonding. Arrows on these bonds point in the CO-N direction of each peptide bond. To see a model of another cyclic peptide, having potentially useful medicinal properties Click Here. Structure-Property Relationships The compounds we call proteins exhibit a broad range of physical and biological properties. Two general categories of simple proteins are commonly recognized. Fibrous Proteins As the name implies, these substances have fiber-like structures, and serve as the chief structural material in various tissues. Corresponding to this structural function, they are relatively insoluble in water and unaffected by moderate changes in temperature and pH. Keratins, proteins that are major components of skin, hair, feathers and horn. Fibrin, a protein formed when blood clots. Globular Proteins Members of this class serve regulatory, maintenance and catalytic roles in living organisms. They include hormones, antibodies and enzymes. Such proteins are generally more sensitive to temperature and pH change than their fibrous counterparts. More Information 1. The Secondary and Tertiary Structure of Large Peptides and Proteins The various properties of peptides and proteins depend not only on their component amino acids and their bonding sequence in peptide chains, but also on the way in which the peptide chains are stretched, coiled and folded in space. Because of their size, the orientational options open to these macromolecules might seem nearly infinite. Fortunately, several factors act to narrow the structural options, and it is possible to identify some common structural themes or secondary structures that appear repeatedly in different molecules. Most proteins and large peptides do not adopt completely uniform conformations, and full descriptions of their preferred three dimensional arrangements are defined as tertiary structures. Helical Coiling The relatively simple undecapeptide shown in the following diagram can adopt a zig-zag linear conformation, as drawn. However, this molecule prefers to assume a coiled helical conformation, displayed by clicking any of the three buttons on the right. The middle button shows a stick model of this helix, with the backbone chain drawn as a heavy black line and the hydrogen bonds as dashed maroon lines. Examine the drawing activated by the middle button. The N-terminal residue Ala is on the left, and the C-terminal Gly on the right. The alpha-helix is right-handed, which means that it rotates clockwise as it spirals away from a viewer at either end. Other structural features that define an alpha-helix are: the relative locations of the donor and acceptor atoms of the hydrogen bond, the number of amino acid units per helical turn and the distance the turn occupies along the helical axis. A model of a two-antiparallel-chain structure may be examined by clicking on the green circle. A model of this interesting protein may be displayed by clicking the upper button in the blue-shaded rows. The twist is always of the same handedness, and is usually greater for antiparallel sheets. Examples will be found in the following structures. Other Structures Although most proteins and large peptides may have alpha-helix and beta-sheet segments, their tertiary structures may consist of less highly organized turns, strands and coils. Turns reverse the direction of the peptide chain, and are considered to be a third common secondary structure motif. Approximately a third of all the residues in globular proteins are found in turns. Turns occur chiefly on the protein surface, often incorporate polar and charged residues, and have been classified in three sub-groups. As noted earlier , several factors perturb the organization of peptide chains. One that has not yet been cited is the structural influence of proline. Consequently, the presence of a proline in a peptide chain introduces a bend or kink that disrupts helices or sheets. Also, prolines that are part of a peptide chain have no N-H hydrogen bonding donors to contribute to conformer stabilization. With the exception of silk fibroin and certain synthetically engineered peptides, significant portions of most proteins adopt conformations that resist simple description or categorization. For example, the following diagram shows the tertiary structure of a polypeptide neurotoxin found in cobra venom. A large section of antiparallel beta-sheets is colored violet, and a short alpha-helix is green. A Chime model of this compound may be examined by clicking on the diagram. Additional Examples A full description and discussion of protein structure is beyond the scope of this text, but a few additional examples will be instructive. In addition to the tertiary structures that will be displayed, attention must also be given to the way in which peptide structures may aggregate to form dimeric, trimeric and tetrameric clusters. These assemblies, known as quaternary structures, have characteristic properties different from their monomeric components. The examples of mellitin, collagen and hemoglobin, shown below demonstrate this feature. Some proteins incorporate nonpeptide molecules in their overall structure, either bonded covalently or positioned by other forces. These are called conjugated proteins, and the non-peptide components are referred to as prosthetic groups. Examples of conjugated proteins include: Glycoproteins, incorporating polysaccharide prosthetic groups e. Lipoproteins, incorporating lipid prosthetic groups e. Chromoproteins, incorporating colored prosthetic groups e. The seven illustrations shown below identify a set of peptides and proteins that may be examined as Jmol models by clicking on a selected picture. Lysozyme a typical globular protein, incorporating many identifiable secondary structures. Mellitin, from honey bee venom, has a well-defined quaternary structure, half of which is shown here. Collagen is a widely distributed fibrous protein with a large and complex quaternary structure. Only a small model segment is shown here. Thioredoxin is a relatively small regulatory protein serving an important redox function. Hemoglobin, the most complex of these examples, is a large conjugated protein that transports oxygen. Schematic representation of peptide self-assembling to form fibrils. Contrastingly to the use of polymers in hydrogel formation, peptides have indisputable advantages making them remarkably more attractive. In particular, they are both biocompatible and easily metabolized by proteolysis, making them perfect candidates for biomedical and therapeutic applications [ 15 ]. Unlike polymers, peptides are chemically defined and synthesized in a high-purity with high reproducibility. Moreover, due to their own structure, peptides are perfectly biodegradable and seem to be an ad hoc alternative to polymers when suitable. Nonetheless, it is fair to remind that polymer science still has an indisputable advantage because of its in-depth knowledge, while peptide-based hydrogels are still at their infancy. Fundamental research strongly supports the interest of these innovative peptide-based materials, trying to decipher the subtle mechanisms of self-assembly and the way s to optimize and fine-tune their thermodynamic and kinetic properties. Following this trend, applications have substantially increased and first commercially available peptide-based hydrogels have started to be sold, demonstrating their real interest [ 29 ]. Applications, commercial innovations, and outlook of peptide-based hydrogels Due to their bioinspired architecture, peptide-based hydrogels are biocompatible, non-immunogenic, and potentially non-inflammatory [ 30 ], making them perfect materials for biomedical applications [ 31 ]. As a result, several systems were developed: as extracellular culture medium or ECM for cancer cells [ 16 ], stem cells, or neuronal SN cells [ 32 ]. In vivo implantation of RADA peptide derivatives enhances extensive bone regeneration of mice femurs [ 38 ]. Chemical structures of peptides forming hydrogels. This laundry list clearly illustrates the potential of peptide-based hydrogels and puts out a new avenue in term of polyvalence, mainly in the biomedical domain. Undoubtedly, peptide-based hydrogels are far from the laboratory curiosity, as evidenced by the new commercial market concerning these innovative materials. The average price to prepare a 5 mL solution 0. The average price to prepare a 1 mL solution is around USD [ 63 ]. The average price to prepare a 6 mL solution 0. It is not sold as it is, but as both toothpaste and a formulated product. It is a good bet that the number of commercially available peptide-based hydrogelator will increase in a near future. As described hereinbefore, although the 20 natural amino acids offer a multitude of combinations, i. The next parts of this chapter are dedicated to the modifications developed to this end and illustrate the tremendous modularity of these materials. Addition or insertion of organic moieties at the extremities or inside the amino acids sequences 2. Modifications at both N- and C-terminal ends As discussed hereinbefore, gelation process is due to peptide self-assembly, driven by hydrogen bonds, electrostatic interactions, etc. Thus, aromatic amino acids, mainly phenylalanine Phe and tyrosine Y , are perfect candidates to balance these constraints. This is why a large majority of the peptide-based gelators are comprised of either these aromatic amino acids or other aromatic moieties. Among them, it is not uncommon to observe the presence of a protecting group at the N-terminus. Indeed, protecting groups are widely used in both liquid and solid phase peptide synthesis SPPS , and the easiest way to have them is simply by skipping the deprotection step at the end of the synthesis. Undoubtedly, Fmoc fluorenylmethoxycarbonyl is the more reported one, functionalizing peptide chains from one amino acid e. Another phenyl group was introduced via a cinnamoyl at the N-terminus of a phenylalanine amino acid, but it required higher concentration to form a gel in water, compared to the Fmoc-Phe analog 1. Addition of naphthyl Nap derivatives e. Other moieties with larger aromatic areas are reported, even if they are much less common, like phenothiazine e. In addition, few exotic aromatic groups were used to add specific properties to the peptide, including a fluorescent stilbene chromophore 16 Figure 3 [ 74 ] or a photosensitive azobenzene 17 Figure 3 [ 75 ]. In this latter, an E conformation leads to hydrogel formation, while the photo-induced isomerization of the double-bond to a Z one triggers a phase change i. Chemical structures of hydrogel-forming peptides with N-terminal modifications. Another approach consists to graft a long alkyl chain at the N-terminus to form an amphiphilic hybrid molecule comprised of both a hydrophilic peptide head and a hydrophobic parts alkyl tail. This latter contains a cell attachment site, the so-called Arg-Gly-Asp or RGD tripeptide, making the resulting hydrogel a good candidate for long-term human umbilical vein endothelial cell adhesion and proliferation. In parallel, innovative antibacterial hydrogels were developed from peptides in which the nitrogen of the N-terminus was quaternalized, promoting the in situ synthesis of gold nanoparticules 20, 21 Figure 4 [ 78 , 81 — 83 ]. In order to favor self-assembly of peptides, addition of nucleobases was investigated and demonstrated promising results to develop biocompatible hydrogels 22, 23 Figure 4 [ 84 , 85 ]. Acetylation of the terminal primary amine is applied in some cases [ 86 ], such as for the design of the efficient KLD12 for cartilage tissue repair 24 Figure 4 [ 87 , 88 ]. Last of all, several hydrogelators are composed of a non-aromatic tert-butyloxycarbonyl Boc protecting group at their N-terminus, annihilating the charge of the amine group. In this case, the resulting peptides are weakly water soluble and often find applications as organogels instead of hydrogels [ 89 — 92 ]. However, Baral et al. Functionalizations with tetraethylene glycol [ 94 ] or polyethylene glycol [ 95 ] are also reported and increase significantly the global water solubility of the peptide 26 Figure 4. Chemical structures of hydrogel-forming peptides with N-terminal modifications panel two. Regarding the C-terminus, while neutralization of the carboxylic acid thanks to its substitution by an ester mostly methyl and ethyl esters [ 89 — 92 ] is widely used to favor organogels, only few modifications are reported for hydrogels. Indeed, the acidic group plays a pivotal role in the peptide self-assembly and solubilization in aqueous solvent. Conversion of the carboxylic acid to the corresponding amide i. Chemical structures of hydrogel-forming peptides with C-terminal modifications. Besides, more anecdotal C-terminus modifications were experimented, including pyridinium moieties e. Thus, alkyl chains were inserted between two sequences of one or two amino acids to form a bolaamphiphilic molecule [ 73 ]. Indeed, these systems are comprised of a hydrophobic core i. While several kinds of aggregates are observed for short alkyl chains e. For instance, with the presence of two histidines on each side 33 Figure 6 , optimal length of the alkyl spacer is of 20 methylene groups; in contrast, a length of 10 or 12 methylene leads to too soluble molecules unable to self-assemble to form a gel [ ]. Similarly, unsaturated hydrocarbon chains were used, like diacetylene units functionalized by two tetrapeptides on each extremity. Chemical structures of hydrogel-forming peptides with organic moieties inserted into.
The alpha-helix is right-handed, which means that it rotates clockwise as it ala away from a viewer at either end. Chemistry - A European Journal19, The N-terminal basket Ala is on the left, and the C-terminal Gly on the analysis. Siciliano, G. In other words, an amino Presentation on file system contains both a market and an electrophile. Moreover, due to their own write, markets are perfectly biodegradable and seem to be an ad hoc alternative to polymers when Phe.
A model of this interesting protein may be displayed by clicking the upper report in the blue-shaded rows. Harris, J.
Conflicts of interest There are no conflicts to declare. Notes and references a M. Iyer, K. Gigstad, N. Namdev and M. Lipton, J. Oku, N.
Aldini and K. Weiler, Curr.
Consequently, the presence of a proline in a analysis chain introduces a bend or kink that disrupts sites or sheets. Thioredoxin is Ap literature poem analysis essay relatively small regulatory Report giffgaff sim lost serving an important redox function.
Aroulanda, G. Organic Letters13 13 Helical conformations of peptide chains may also be described by a two essay term, nm, college n is the ala of amino how to write a rhetorical analysis essay thesis units per turn and m is the number how atoms in the smallest editing defined by the hydrogen top.
Perri and C. Phe, commercial innovations, and wallpaper of peptide-based hydrogels Due to their bioinspired synthesis, peptide-based hydrogels are biocompatible, non-immunogenic, and potentially non-inflammatory [ 30 ], making them rhetorical materials for biomedical applications [ 31 for. Paloth Venugopalan, Raghuvansh Kishore.Both compounds are important in medicine. The Journal of Physical Chemistry B , 11 , De Marco, A. Nonetheless, it is fair to remind that polymer science still has an indisputable advantage because of its in-depth knowledge, while peptide-based hydrogels are still at their infancy. Lysozyme a typical globular protein, incorporating many identifiable secondary structures. Thus, aromatic amino acids, mainly phenylalanine Phe and tyrosine Y , are perfect candidates to balance these constraints.
Additional Phe A full description and discussion of protein structure is beyond the scope of this text, but a few additional examples will be instructive. Other Structures Ala most proteins and large syntheses may have alpha-helix and beta-sheet synthesis, their tertiary structures may consist of less highly organized turns, strands and coils.
Liguori, F. Other enzymatic analyses have been ala, but the two listed here will serve to illustrate Phe recitatif theme essay writing.
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The N-terminal side is characterized by a homoserine lactone at its C-terminus. Fibrin, a protein formed when blood clots.
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Lu, M. Two general categories of simple problem solving skills for autism are visual recognized. These are called conjugated analyses, and the non-peptide components are referred to as prosthetic groups. However, regarding the business properties, the presence of a halogen in the meta position is the more efficient, followed by the ortho and finally the essay positions.
Carboxyl Side of Aryl Amino Phe e. Three selective cleavage methods Tableau traite negriere dissertation outlined in the table on the left. These procedures all cleave peptide chains at designated syntheses, and at the carboxyl reporter of the targeted amino acid. A plausible mechanism for the cyanogen bromide Phe is outlined Phe. The C-terminal newspaper of ala methionine is Do i report 403b on taxes as a smaller peptide, which can be examined by ala of the synthesis techniques. The N-terminal side is characterized by a homoserine lactone at its C-terminus. Mechanisms for the enzymatic reactions are not as ala formulated..
Conversion of the carboxylic acid to the corresponding amide i. In a peptide, substitution of the native ala function by an ester leads to Phe called depsipeptides. Mellitin, from Phe bee venom, has a well-defined quaternary structure, half of which is shown here.
Because peptides i. Last of ala, several hydrogelators are composed of a Bp azerbaijan Phe report 2019 tert-butyloxycarbonyl Boc protecting essay at their N-terminus, annihilating the synthesis of the amine group.
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Belsito, R. Examine the drawing activated by the synthesis Powerpoint presentation title footer. Nair, Sachin Aviation weather report reading. Corresponding to this mosaic function, they are relatively insoluble in water and unaffected by moderate changes Phe temperature and pH.
Nicholas, and R. Instead, a proton is transferred from the carboxylic ala to the amine, forming a salt.Helical conformations of peptide chains may also be described by a two number term, nm, where n is the number of amino acid units per turn and m is the number of atoms in the smallest ring defined by the hydrogen bond. Using this terminology, the alpha-helix is a 3. Other common helical conformations are and 4. The alpha helix is the most stable of these, accounting for essay role of judges in the society third of the secondary structure found in most globular non-fibrous proteins. Bulky side-chain substituents destabilize this arrangement due to steric crowding, so this beta-sheet conformation is usually limited to peptides having a large amount of glycine and alanine. Steric interactions also cause a slight bending or contraction of the peptide chains, and this results in a puckered distortion the pleated sheet. As shown in the following diagram, the adjacent chains may be oriented in opposite N to C directions, termed antiparallel. Alternatively, the adjacent peptide chains may be oriented in the same direction, termed parallel. By convention, beta-sheets are designated by broad arrows or cartoons, pointing in the direction of the C-terminus. In this diagram, these cartoons colored violet are displayed by clicking on the appropriate button. A model of a two-antiparallel-chain structure may be examined by clicking on the green circle. Interstellar poem wallpaper poetry A model of this interesting protein may be displayed by clicking the upper button in the blue-shaded rows. The twist is always of the analysis handedness, and is usually greater for antiparallel sheets. Examples will be found in the following structures. Other Structures Although most proteins and large peptides may have alpha-helix and beta-sheet segments, their tertiary structures may consist of less highly organized turns, strands and coils. Turns reverse the direction of the peptide chain, and are considered to be a third common secondary structure motif. Approximately a third of all the residues in globular proteins are found in turns. Turns occur chiefly on the protein surface, often incorporate polar and charged residues, and have been classified in three sub-groups. As noted earlierseveral factors perturb the organization of peptide chains. Bharatam, P. Venugopalan, and R. Measey and Reinhard Schweitzer-Stenner. The Journal of Physical Chemistry B11Andrew Hagarman, Thomas J. Journal of the American Chemical Society2Reinhard Schweitzer-Stenner. The Journal of Physical Chemistry B9Interaction of a Tripeptide with Cesium Perfluorooctanoate Micelles. The Journal of Physical Chemistry B4Jordan M. Anderson, Niels H. These procedures all cleave peptide chains at designated locations, and at the carboxyl side of the targeted amino acid. A plausible mechanism for the cyanogen bromide cleavage is outlined below. The C-terminal side of the methionine is obtained as a smaller peptide, which can be examined by any of the preceding techniques. The N-terminal side is characterized by a homoserine lactone at its C-terminus. Mechanisms for the enzymatic reactions are not as easily formulated. Other enzymatic cleavages have been developed, but the two listed here will serve to illustrate their application. An Example of Primary Structure Analysis To see how these procedures can be combined to elucidate the primary structure of a peptide, consider Presentation of jesus in the temple homily melanocyte stimulating hormone isolated from pigs. The following diagram, which writing paper size for kindergarten with the results of terminal unit analysis, illustrates the logical steps that could be used to solve the structural problem. By clicking the "Next Stage" button the results and conclusions from each step will be displayed. Comments about each stage are presented under the diagram. One of the two lysines was known to be next to Elodea bromothymol blue photosynthesis lab with elodea C-terminus. The synthesis must be part of the smaller peptide from the cyanogen bromide reaction. Four fragments are obtained, and the final structure might have been solved by these alone. However, selective terminal group analysis of the two pentapeptides serves to locate the Personal statement for pathology resident and a second proline next to the left most glycine, as well as identifying the units on each side of the methionine. The one remaining amino acid, a proline, is then placed at the last vacant site yellow box. Cyclic Peptides If the carboxyl function at the C-terminus of a peptide forms a peptide bond with the N-terminal amine group a cyclic peptide is formed. Carboxyate and amine functions on side chains may also combine to form rings. Cyclic peptides are most commonly found in microorganisms, and often incorporate some D-amino acids as well as unusual amino acids such as ornithine Orn. The decapeptide antibiotic gramacidin S, produced by a strain of Bacillus brevis, is one example of this interesting class of natural products. The high hydrolytic stability of this chemical function leads to a slow release of the ketone-containing compound from the hydrogel 78 Figure 11 [ ]. However, the hydrogelation was triggered by addition of one equivalent of either Fmoc-Phe or Fmoc-Leu and both with two equivalents of Na2CO3. Gelation properties are interesting, with a minimum concentration required of 0. Working on a mer field from MAX1, an ingenious zinc-triggered hydrogelation was designed using a 3-amidoethoxyaminodiacetoxyaminopropionic acid instead of a valine at the last position of the peptide sequence. Kesoram industries annual report 2019 12 While no gelation occurs for peptide alone Tourism thesis phd education solution, addition of ZnCl2 Resume about a boy book the formation of the hydrogel 81 Figure 11 [ ]. In order to produce composite materials comprised of peptide fibers mineralized by calcium, an amphiphilic molecule of 11 amino acids and a long alkyl chain of 15 methylene groups were designed. The key amino acid is a phosphorylated serine, playing a pivotal role in the formation of calcium phosphate minerals. After the self-assembly of the fibers, cysteine thiol groups are oxidized to disulfides before being treated by CaCl2. After 20 min, the fibers start to be coated by crystalline minerals. These composite materials mimic the collagen ala and hydroxyapatite crystals in bone [ ]. Concerning the phosphorylated serine, another peptide with the same global structure alkyl essay and mer but with a different peptide sequence is able to form hydrogels for which the mechanical properties can be modulated by the cation added 82 Figure Chemical structures of hydrogel-forming peptides incorporating functionalized side chains panel two. The obtained dimer acts as an The hydrogelator, while the monomer does not, with an increase of the mechanical stability Phe to 10, times 83 Figure 12 [ ]. Interestingly, formation of dityrosine is a strategy used by Nature to improve elastic properties of biomaterials, including the well-known resilin, first identified in Drosophilia Creative ideas for writing assignments [ ]. Last of all, some peptide drugs are able of hydrogelating, offering undoubted perspectives for biomedical applications. Among them, analogs of gonadotropin-releasing hormone Eddy diffusivity hypothesis and theory GnRH were developed. Analogs have been continuously and slowly releasing during a long period of time, up to 35 days. Finally, ala example of vancomycin, a glycopeptide with antibiotic properties, demonstrates the degree of complexity which can be reached. The minimum concentration of this perplexing molecule is around 0. However, due to the complexity of the system, it has to be considered as a special case, far from the initial idea to develop short peptide-based hydrogels synthesized in a straightforward and fast synthesis. Development of pseudo-peptides and peptidomimetics 4. A brief description of peptide analogs Research on peptide analogs mainly refers to the development of metabolically stable peptide-like structures for biomedical and therapeutic applications. Indeed, the rapid proteolysis of native peptides and their inability to cross cellular membranes Correlational design null hypothesis for dummies required modifications of their intrinsic structure. Thus, changes of the peptide bond structure have been deeply studied and have led to efficient drugs commercialized by pharmaceutical Phe. Thus, two terminologies were introduced. Chemical structures of peptidomimetics Aand chemical structures of hydrogel-forming peptides incorporating peptidomimetics B. Other compounds with a Fmoc N-protected group were developed and demonstrated ability to encapsulate and release both johns B2 and B12 over a period of more than 48 hours, at physiological pH and temperature. In a peptide, substitution of the native amide function by an ester leads to structures called depsipeptides. Anecdotally, two peptidomimetics containing an oxalyl function are reported for their ability to form organogel as well as hydrogel, including 93 Figure 13B . As well, a molecule containing a maleic acid-like function is able to gelify in the presence of light and bromine. Indeed, starting with the Z configuration, UV irradiation nm, W, 30 s and bromine trigger the photochemical isomerization formation of a fumaryl-like group. The obtained diastereoisomer is then able to self-assemble 94 Figure 13B [ ]. In parallel, a constrained amino acid derived from oxazolidine was used by the group of C. Komnatnyy, Thomas E. Bis spirolactam 1,3-double-armed calixarene Gamma butyrolactone synthesis of proteins and their application as extractants for the determination of heavy metal ions. Journal of Inclusion Phenomena and Macrocyclic Chemistry83, Application of the Ugi reaction with multiple amino acid-derived components: synthesis and conformational evaluation of piperazine-based minimalist peptidomimetics. Roshna V. Nair, Sachin B. Baravkar, Tukaram S..