Destabilization of the 310-Helix in Peptides Based on Cα-Tetrasubstituted α-Amino Acids by Main-Chain to Side-Chain Hydrogen Bonds

1998 ◽  
Vol 120 (45) ◽  
pp. 11558-11566 ◽  
Author(s):  
Wojciech M. Wolf ◽  
Marcin Stasiak ◽  
Miroslav T. Leplawy ◽  
Alberto Bianco ◽  
Fernando Formaggio ◽  
...  
Keyword(s):  
Amino Acids ◽  
Hydrogen Bonds ◽  
Main Chain ◽  
Side Chain ◽  
310 Helix

scholarly journals Side chain to main chain hydrogen bonds stabilize a polyglutamine helix in a transcription factor

2019 ◽  
Vol 10 (1) ◽  
Author(s):  
Albert Escobedo ◽  
Busra Topal ◽  
Micha B. A. Kunze ◽  
Juan Aranda ◽  
Giulio Chiesa ◽  
...  
Keyword(s):  
Transcription Factor ◽  
Hydrogen Bonds ◽  
Main Chain ◽  
Side Chain

Two phosphonodehydrotripeptides: Boc0–Gly1–Δ(Z)Phe2–α-Abu3PO3Me2and Boc0–Gly1–Δ(Z)Phe2–α-Nva3PO3Et2

2013 ◽  
Vol 69 (3) ◽  
pp. 277-281 ◽  
Author(s):  
Anna Brzuszkiewicz ◽  
Maciej Makowski ◽  
Marek Lisowski ◽  
Elżbieta Lis ◽  
Marta Otręba ◽  
...  
Keyword(s):  
Amino Acids ◽  
Hydrogen Bonds ◽  
Crystal Structures ◽  
Main Chain ◽  
Intermolecular Hydrogen Bonds ◽  
Intramolecular Hydrogen Bonds ◽  
Crystal Forms ◽  
Intramolecular Hydrogen

The present paper reports the crystal structures of two short phosphonotripeptides (one in two crystal forms) containing one ΔPhe (dehydrophenylalanine) residue, namely dimethyl (3-{[tert-butoxycarbonylglycyl-α,β-(Z)-dehydrophenylalanyl]amino}propyl)phosphonate, Boc0–Gly1–Δ(Z)Phe2–α-Abu3PO3Me2, C21H32N3O7P, (I), and diethyl (4-{[tert-butoxycarbonylglycyl-α,β-(Z)-dehydrophenylalanyl]amino}butyl)phosphonate, Boc0–Gly1–Δ(Z)Phe2–α-Nva3PO3Et2, as the propan-2-ol monosolvate 0.122-hydrate, C24H38N3O7P·C3H8O·0.122H2O, (II), and the ethanol monosolvate 0.076-hydrate, C24H38N3O7P·C2H6O·0.076H2O, (III). The crystals of (II) and (III) are isomorphous but differ in the type of solvent. The phosphono group is linked directly to the last Cαatom in the main chain for all three peptides. All the amino acids aretranslinked in the main chains. The crystal structures exhibit no intramolecular hydrogen bonds and are stabilized by intermolecular hydrogen bonds only.

scholarly journals Glutamine Side-Chain to Main Chain Hydrogen Bonds Can be used to Design Single Alpha-Helices that are Stable at Room Temperature

2020 ◽  
Vol 118 (3) ◽  
pp. 369a-370a
Author(s):  
Albert Escobedo ◽  
Busra Topal ◽  
Micha Kunze ◽  
Juan Aranda ◽  
Giulio Chiesa ◽  
...  
Keyword(s):  
Hydrogen Bonds ◽  
Room Temperature ◽  
Main Chain ◽  
Side Chain ◽  
Alpha Helices

scholarly journals Anti-cancer peptides: classification, mechanism of action, reconstruction and modification

Open Biology ◽  
2020 ◽  
Vol 10 (7) ◽  
pp. 200004
Author(s):  
Mingfeng Xie ◽  
Dijia Liu ◽  
Yufeng Yang
Keyword(s):  
Amino Acids ◽  
Cell Proliferation ◽  
Drug Resistance ◽  
Mechanism Of Action ◽  
Main Chain ◽  
Side Chain ◽  
Short Peptides ◽  
Anti Cancer ◽  
Cancer Activity ◽  
Tumour Blood

Anti-cancer peptides (ACPs) are a series of short peptides composed of 10–60 amino acids that can inhibit tumour cell proliferation or migration, or suppress the formation of tumour blood vessels, and are less likely to cause drug resistance. The aforementioned merits make ACPs the most promising anti-cancer candidate. However, ACPs may be degraded by proteases, or result in cytotoxicity in many cases. To overcome these drawbacks, a plethora of research has focused on reconstruction or modification of ACPs to improve their anti-cancer activity, while reducing their cytotoxicity. The modification of ACPs mainly includes main chain reconstruction and side chain modification. After summarizing the classification and mechanism of action of ACPs, this paper focuses on recent development and progress about their reconstruction and modification. The information collected here may provide some ideas for further research on ACPs, in particular their modification.

scholarly journals The AAA ATPase Vps4 binds ESCRT-III substrates through a repeating array of dipeptide-binding pockets

eLife ◽  
2017 ◽  
Vol 6 ◽  
Author(s):  
Han Han ◽  
Nicole Monroe ◽  
Wesley I Sundquist ◽  
Peter S Shen ◽  
Christopher P Hill
Keyword(s):  
Hydrogen Bonds ◽  
Main Chain ◽  
Substrate Binding ◽  
Conveyor Belt ◽  
Side Chain ◽  
Peptide Substrate ◽  
Aaa Atpase ◽  
Membrane Fission ◽  
Wide Range ◽  
Binding Pockets

The hexameric AAA ATPase Vps4 drives membrane fission by remodeling and disassembling ESCRT-III filaments. Building upon our earlier 4.3 Å resolution cryo-EM structure (<xref ref-type="bibr" rid="bib29">Monroe et al., 2017</xref>), we now report a 3.2 Å structure of Vps4 bound to an ESCRT-III peptide substrate. The new structure reveals that the peptide approximates a β-strand conformation whose helical symmetry matches that of the five Vps4 subunits it contacts directly. Adjacent Vps4 subunits make equivalent interactions with successive substrate dipeptides through two distinct classes of side chain binding pockets formed primarily by Vps4 pore loop 1. These pockets accommodate a wide range of residues, while main chain hydrogen bonds may help dictate substrate-binding orientation. The structure supports a ‘conveyor belt’ model of translocation in which ATP binding allows a Vps4 subunit to join the growing end of the helix and engage the substrate, while hydrolysis and release promotes helix disassembly and substrate release at the lagging end.

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