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Small Peptides for Inhibiting Serum Amyloid A Aggregation.
Jana, Asis K; Greenwood, Augustus B; Hansmann, Ulrich H E.
  • Jana AK; Department of Chemistry & Biochemistry, University of Oklahoma, Norman, Oklahoma 73019, United States.
  • Greenwood AB; Department of Chemistry & Biochemistry, University of Oklahoma, Norman, Oklahoma 73019, United States.
  • Hansmann UHE; Department of Chemistry & Biochemistry, University of Oklahoma, Norman, Oklahoma 73019, United States.
ACS Med Chem Lett ; 12(10): 1613-1621, 2021 Oct 14.
Article in English | MEDLINE | ID: covidwho-1483085
ABSTRACT
Deposition of human serum amyloid A (SAA) amyloids in blood vessels, causing inflammation, thrombosis, and eventually organ damage, is commonly seen as a consequence of certain cancers and inflammatory diseases and may also be a risk after SARS-COV-2 infections. Several attempts have been made to develop peptide-based drugs that inhibit or at least slow down SAA amyloidosis. We use extensive all-atom molecular dynamic simulations to compare three of these drug candidates for their ability to destabilize SAA fibrils and to propose for the best candidate, the N-terminal sequence SAA1-5, a mechanism for inhibition. As the lifetime of peptide drugs can be increased by replacing l-amino acids with their mirror d-amino acids, we have also studied corresponding d-peptides. We find that DRI-SAA1-5, formed of d-amino acids with the sequence of the peptide reversed, has similar inhibitory properties compared to the original l-peptide and therefore may be a promising candidate for drugs targeting SAA amyloidosis.

Full text: Available Collection: International databases Database: MEDLINE Type of study: Prognostic study Language: English Journal: ACS Med Chem Lett Year: 2021 Document Type: Article Affiliation country: Acsmedchemlett.1c00456

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Full text: Available Collection: International databases Database: MEDLINE Type of study: Prognostic study Language: English Journal: ACS Med Chem Lett Year: 2021 Document Type: Article Affiliation country: Acsmedchemlett.1c00456