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Interaction of Human C5a with the Major Peptide Fragments of C5aR1: Direct Evidence in Support of "Two-Site" Binding Paradigm

ACS Omega. 2021-08; 
Aurosikha Das, Lalita Mohan Behera, Soumendra Rana
Products/Services Used Details Operation
GenParts™ DNA Fragments Total four peptides belonging to the extracellular surface of C5aR1, involving the two major peptide fragments (i) the N-terminus and (ii) the extracellular loop-2 (ECL2), were synthetically prepared using the standard Fmoc chemistry over solid phase by recruiting the services of GenScript (NJ, USA) Get A Quote

摘要

The C5a receptor's (C5aR1) physiological function in various tissues depends on its high-affinity binding to the cationic proinflammatory glycoprotein C5a, produced during the activation of the complement system. However, an overstimulated complement can quickly alter the C5a-C5aR1 function from physiological to pathological, as has been noted in the case of several chronic inflammation-induced diseases like asthma, lung injury, multiorgan failure, sepsis, and now COVID-19. In the absence of the structural data, the current study provides the confirmatory biophysical validation of the hypothesized "two-site" binding interactions of C5a, involving (i) the N-terminus (NT) peptide ("Site1") and (ii) the extracellu... More

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