1. Oostatic peptides
Jan Hlaváček Amino Acids. 2013 Apr;44(4):1095-105. doi: 10.1007/s00726-012-1449-x. Epub 2013 Jan 8.
Oostatic peptides are organic molecules, which influence an insect reproduction due to a regulation of the eggs development. It was proved that decapeptide-H-Tyr-Asp-Pro-Ala-Pro-Pro-Pro-Pro-Pro-Pro-OH (YDPAPPPPPP)-isolated from mosquito Aedes aegypti, inhibits trypsin activity in the midgut of the mosquito. Therefore, it was named trypsin-modulating oostatic factor (Aea-TMOF). Feeding the recombinant cells with cloned and expressed TMOF on the coat protein of tobacco mosaic virus (TMV) to mosquito larvae, caused larval mortality. The TMOF was therefore designed for usage as a new biorational insecticide against mosquito. Similarly, a hexapeptide-H-Asn-Pro-Thr-Asn-Leu-His-OH (NPTNLH)-was isolated from the grey flesh fly Neobellieria bullata. This peptide and some of its analogs inhibited trypsin-like synthesis by the midgut in female flies and was therefore entitled Neb-TMOF. Interestingly, the synthetic Aea-TMOF and mainly its C-terminus shorten analogs, including those containing D-amino acids or methylene-oxy isosteric bond, quickly and strongly inhibited the hatchability and egg development in the flesh fly N. bullata.
2. Visible-Light Microscopic Discovery of Up to 150 μm Long Helical Amyloid Fibrils Built of the Dodecapeptide H-(Val-Ala-Leu)4 -OH and of Decapeptides Derived from Insulin
Monika Świontek, Zbigniew J Kamiński, Beata Kolesińska, Dieter Seebach Chem Biodivers. 2016 Sep;13(9):1111-1117. doi: 10.1002/cbdv.201600167. Epub 2016 Aug 31.
In the formation of amyloid fibrils from small peptides, the appearance of superhelices of (P)- or (M)-helicity has been observed for the first time; high concentrations of the peptides and extended periods of incubation at physiological pH appear to be important for this phenomenon. In view of the general importance of peptide and protein aggregation, we give a brief overview with selected examples for demonstration.
3. Molecular structures of two crystalline forms of the cyclic heptapeptide antibiotic ternatin, cyclo[-beta-OH-D-Leu-D-Ile-(NMe)Ala-(NMe)Leu-Leu-(NMe)Ala-D-(NMe)Ala-]
R Miller, N M Galitsky, W L Duax, D A Langs, V Z Pletnev, V T Ivanov Int J Pept Protein Res. 1993 Dec;42(6):539-49. doi: 10.1111/j.1399-3011.1993.tb00362.x.
The crystal structures of two solvated forms of ternatin, cyclo[-beta-OH-D-Leu-D-Ile-(NMe)Ala-(NMe)Leu-Leu-(NMe)Ala-D-(NMe)Ala-] are reported. The first crystallizes with two molecules of peptide and one of dioxane in the asymmetric unit: P2(1)2(1)2(1), a = 11.563(1), b = 21.863(2), c = 36.330(4) A. The second crystallizes with two molecules of peptide and one of water in the asymmetric unit: P2(1)2(1)2(1), a = 14.067(2), b = 16.695(1), c = 36.824(6) A. N-Methylation of four of the seven residues of ternatin appears to reduce the number of low-energy conformations the molecule can assume. The same H-bonded macrocyclic ring conformation is adopted by the backbone of each of the four molecules observed here. All the amino-acid side chains, with the exception of D-Ile2, have similar orientations in each of the four conformers. The heptapeptide macrocycle is characterized by: (i) a cis peptide between (NMe)Ala3 and (NMe)Leu4, (ii) a type II beta-bend, involving residues Leu5-(NMe)Ala6-D-(NMe)Ala7-beta-OH-D-Leu1, stabilized by two H-bonds, N1-->O5 and N5-->O1, between Leu5 and beta-OH-D-Leu1 residues, (iii) a third intramolecular H-bond, observed in each of the four molecules, between the hydroxyl group of beta-OH-D-Leu1 and the carbonyl oxygen of D-Ile2.
