Detection of target collagen peptides with single amino acid mutation using two fluorescent peptide probes

2019 ◽  
Vol 7 (48) ◽  
pp. 7676-7682
Author(s):  
Xiuxia Sun ◽  
Linyan Yao ◽  
Caihong Fu ◽  
Liting Luo ◽  
Jie Wang ◽  
...  
Keyword(s):  
Amino Acid ◽  
Single Amino Acid ◽  
Amino Acid Mutation ◽  
Collagen Peptides ◽  
Fluorescent Peptide ◽  
Peptide Probes ◽  
First Time ◽  
Single Amino Acid Mutation ◽  
Quenching Assay

We have herein for the first time reported the development of a fluorescent self-quenching assay to detect target collagen peptides with a single amino acid mutation.

scholarly journals Prospective mapping of viral mutations that escape antibodies used to treat COVID-19

Science ◽  
2021 ◽  
Vol 371 (6531) ◽  
pp. 850-854 ◽  
Author(s):  
Tyler N. Starr ◽  
Allison J. Greaney ◽  
Amin Addetia ◽  
William W. Hannon ◽  
Manish C. Choudhary ◽  
...  
Keyword(s):  
Amino Acid ◽  
Infected Patient ◽  
Viral Escape ◽  
Single Amino Acid ◽  
Receptor Binding Domain ◽  
Amino Acid Mutation ◽  
The Individual ◽  
Viral Surveillance ◽  
Single Amino Acid Mutation

Antibodies are a potential therapy for severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), but the risk of the virus evolving to escape them remains unclear. Here we map how all mutations to the receptor binding domain (RBD) of SARS-CoV-2 affect binding by the antibodies in the REGN-COV2 cocktail and the antibody LY-CoV016. These complete maps uncover a single amino acid mutation that fully escapes the REGN-COV2 cocktail, which consists of two antibodies, REGN10933 and REGN10987, targeting distinct structural epitopes. The maps also identify viral mutations that are selected in a persistently infected patient treated with REGN-COV2 and during in vitro viral escape selections. Finally, the maps reveal that mutations escaping the individual antibodies are already present in circulating SARS-CoV-2 strains. These complete escape maps enable interpretation of the consequences of mutations observed during viral surveillance.

scholarly journals A Single Amino Acid Mutation (R104P) in the E/DRY Motif of GPR40 Impairs Receptor Function

PLoS ONE ◽  
2015 ◽  
Vol 10 (10) ◽  
pp. e0141303 ◽  
Author(s):  
Shimeng Guo ◽  
Jiandong Zhang ◽  
Shuyong Zhang ◽  
Jing Li
Keyword(s):  
Amino Acid ◽  
Single Amino Acid ◽  
Receptor Function ◽  
Amino Acid Mutation ◽  
Dry Motif ◽  
Single Amino Acid Mutation
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