Amino acids hexapeptide

An example of this strategy is the preparation of a synthetic combinatorial library of hexapeptides. The maximum number of sequence combinations for hexapeptides is 20 or 64,000,000. One approach to simplify preparation and screening possibilities for such a library is to specify the first two amino acids in the hexa-... 

This led to the conclusion that these amino acids were essential for the resolution capability and only 6 new libraries of 18 compounds had to be synthesized with these amino acid residues to define the position 3. Surprisingly, the separation abilities of all six libraries were very similar. Therefore, tyrosine was chosen for continuing deconvolution, since it is convenient as its aromatic ring can easily be detected by UV spectrometry. The last step, defining position 5, required the synthesis and testing of 6 individual hexapeptides. 

Fig. 3-3. Comparison of the values of enantiomeric resolution of different DNP-D,L-amino acids at different deconvolution stages of a cyclic hexapeptide sublibrary. Resolution values in a cyclo(Arg-Lys-X-X-X-P-Ala) sublibrary, in the first line, are compared to those obtained in sublibraries with a progressively increasing number of defined positions. All the sublibraries were 30 mM in the running buffer while the completely defined cyclo(Arg-Lys-Tyr-P-Tyr-P-Ala) peptide is used at 10 mM concentration. Conditions cyclopeptide sublibrary in 20 mM sodium phosphate buffer, pH 7.0 capillary, 50 pm i.d., 65 cm total length, 57 cm to the window V = -20 kV, I = 40 electrokinetic injection, -10 kV, 3 s detection at 340 nm. (Reprinted with permission from ref. [75]. Copyright 1998, American Chemical Society.)...

Give the amino acid sequence of hexapeptides that produce the following sets of fragments on partial acid hydrolysis ... 

This type of yvn-seleclivc aldol addition has been applied in the synthesis of the unusual L-threonine based amino acid, (2,S, 3/ ,6F)-3-hydroxy-4-methyl-2-methylamino-6-octenoic acid, of cyclosporine104, of the cyclic hexapeptide echinocandin105, and of the antibiotic ionomycin97. 

Surprisingly, in contrast to a- and y9-peptides, CD spectra of y-peptides gave only a very hmited amount of stmctural information. Experiments conducted on heh-cal y" -hexapeptides did not reveal any characteristic CD signature (no Cotton effect) [200, 201]. Similarly, y -peptides built from 2,4-disubstituted y-amino acids of like configuration and shown to adopt a more stable 2.6-helical structure, do not display typical CD curves either [201]. However, CD spectra of the 2.6-helical -peptide 147 and its Boc-protected derivative recorded in MeOH and CD3CN present an intense maximum around 215 nm with a shoulder at ca. 200 nm [207]. 

Tropoelastin is the soluble precursor of elastin and consists of alternating hydrophobic and hydrophilic peptide domains. The most common amino acids in the hydrophobic domains are Gly, Val, Ala, and Pro, which are often present in repeats of tetra-, penta-, and hexapeptides, such as Gly-Gly-Val-Pro, Gly-Val-Gly-Val-Pro, Gly-Val-Pro-Gly-Val, and Gly-Val-Gly-Val-Ala-Pro, respectively [3, 4]. The hydrophilic domains are mainly composed of lysines interspersed by alanines. 

B Because it is a hexapeptide and there are five distinct amino acids, one amino acid must appear twice. The fragmentation pattern indicates that the doubled amino acid is glycine. The sequences fall into place if we begin with the N-terminal end. 

The structurally related myxochromides Aj.j are cyclic hexapeptides produced by several Myxococcus species. These examples contain a proline residue, which is not present in myxochromides Si 3, as the fourth amino acid in their peptide core. The NRPSs responsible for myxochromides A and S biosynthesis have exacdy the same module and domain organization thus, the fourth module of the myxochromide S synthetase must be skipped to account for the natural product. Biochemical experiments revealed that the A domain of this module activates L-proline, but the adjacent PCP domain cannot be phosphopantetheinylated by a PPTase. These results suggest that the C domain of module 5 reacts directly with the tripeptide intermediate bound to the PCP domain of module 3 in myxochromide S biosynthesis. A similar example of domain skipping has been noted in the biosynthesis of the mannopeptimycins. ... 

The words peptide and polypeptide are both used to describe chains of amino acids linked by peptide bonds. Peptides are short chains of amino acids that do not form part of a protein. The number of amino acids is indicated by a prefix (e.g. dipeptide, hexapeptide, oligopeptide). Polypeptides (or polypeptide chains) are longer sequences which can form part of a protein, which may consist of several polypeptides (Appendix 3.1). 

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