scholarly journals Modulation of supramolecular self-assembly of an antimicrobial designer peptide by single amino acid substitution: implications on peptide activity

2019 ◽  
Vol 1 (12) ◽  
pp. 4679-4682 ◽  
Author(s):  
Zhou Ye ◽  
Conrado Aparicio

Single amino acid substitution of charged or hydrophobic amino acids of a designer antimicrobial peptide modulated structural and self-assembly performance and potency.

2015 ◽  
Vol 64 ◽  
pp. 116-125 ◽  
Author(s):  
Nathalie Geneix ◽  
Michèle Dalgalarrondo ◽  
Bénédicte Bakan ◽  
Agnès Rolland-Sabaté ◽  
Khalil Elmorjani ◽  
...  

2018 ◽  
Author(s):  
Nidhi Gour ◽  
Bharti Koshti ◽  
Chandra Kanth P. ◽  
Dhruvi Shah ◽  
Vivek Shinh Kshatriya ◽  
...  

We report for the very first time self-assembly of Cysteine and Methionine to discrenible strucutres under neutral condition. To get insights into the structure formation, thioflavin T and Congo red binding assays were done which revealed that aggregates may not have amyloid like characteristics. The nature of interactions which lead to such self-assemblies was purported by coincubating assemblies in urea and mercaptoethanol. Further interaction of aggregates with short amyloidogenic dipeptide diphenylalanine (FF) was assessed. While cysteine aggregates completely disrupted FF fibres, methionine albeit triggered fibrillation. The cytotoxicity assays of cysteine and methionine structures were performed on Human Neuroblastoma IMR-32 cells which suggested that aggregates are not cytotoxic in nature and thus, may not have amyloid like etiology. The results presented in the manuscript are striking, since to the best of our knowledge,this is the first report which demonstrates that even non-aromatic amino acids (cysteine and methionine) can undergo spontaneous self-assembly to form ordered aggregates.


1996 ◽  
Vol 5 (3) ◽  
pp. 542-545 ◽  
Author(s):  
Kunihiko Gekko ◽  
Youjiro Tamura ◽  
Eiji Ohmae ◽  
Hideyuki Hayashi ◽  
Hiroyuki Kagamiyama ◽  
...  

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