63328-06-3Relevant academic research and scientific papers
Potent Antimicrobial Activity of Lipidated Short α,γ-Hybrid Peptides
Benke, Sushil N.,Thulasiram, Hirekodathakallu V.,Gopi, Hosahudya N.
, p. 1610 - 1615 (2017/10/16)
Herein we report the potent antimicrobial activity of α,γ-hybrid lipopeptides composed of 1:1 alternating α- and γ-amino acids. Along with their potent antimicrobial activity against various Gram-positive and Gram-negative bacteria, these hybrid lipopepti
Protein secondary structure mimetics: Crystal conformations of α/γ4-hybrid peptide12-helices with proteinogenic side chains and their analogy with α- And β-peptide helices
Jadhav, Sandip V.,Bandyopadhyay, Anupam,Gopi, Hosahudya N.
supporting information, p. 509 - 514 (2013/03/14)
Numerous strategies have been developed to mimic the α-helical secondary structure using hybrid peptides containing non-natural amino acids. In contrast to the β- and α/β-hybrid peptides, very little is known about the folding patterns of hybrid peptides
A versatile annulation protocol toward novel constrained phosphinic peptidomimetics
Nasopoulou, Magdalini,Georgiadis, Dimitris,Matziari, Magdalini,Dive, Vincent,Yiotakis, Athanasios
, p. 7222 - 7228 (2008/02/12)
(Chemical Equation Presented) The development of a novel 3-center 2-component annulation reaction between α,ω-carbamoylaldehydes and suitably monoalkylated phosphinic acids is reported. Depending on the starting α,ω-carbamoylaldehyde, diverse phosphinic scaffolds varying in the size of their rigidity element, the nature and stereochemistry of substituents, and the participation of heteroatoms in the azacyclic ring system can be obtained in one synthetic step and in high yield. In addition, this methodology allows the synthesis of Fmoc-protected constrained aminophosphinic acids that can be easily converted to suitable pseudodipeptide building blocks compatible with the requirements of peptide synthesis on the solid phase. Finally, the careful choice of both substituents and protecting groups can provide functionally diverse, orthogonally protected constrained scaffolds for extended derivatization of the target phosphinic peptidomimetic structrures.
