A combined spectroscopic and molecular modeling Study on structure-function-dynamics under chemical modification: Alpha-chymotrypsin with formalin preservative

Pritam Biswas, Aniruddha Adhikari, Uttam Pal, Susmita Mondal, Dipanjan Mukherjee, Ria Ghosh, Rami J. Obaid, Ziad Moussa, Sudeshna Shyam Choudhury, Saleh A. Ahmed, Ranjan Das, Samir Kumar Pal

Research output: Contribution to journalArticlepeer-review

2 Citations (Scopus)

Abstract

Enzyme function can be altered via modification of its amino acid residues, side chains and large-scale domain modifications. Herein, we have addressed the role of residue modification in catalytic activity and molecular recognition of an enzyme alpha-chymotrypsin (CHT) in presence of a covalent cross-linker formalin. Enzyme assay reveals reduced catalytic activity upon increased formalin concentration. Polarization gated anisotropy studies of a fluorophore 8-Anilino-1-naphthalenesulfonic acid (ANS) in CHT show a dip rise pattern in presence of formalin which is consistent with the generation of multiple ANS binding sites in the enzyme owing to modifications of its local amino acid residues. Molecular docking study on amino acid residue modifications in CHT also indicate towards the formation of multiple ANS binding site. The docking model also predicted no change in binding behavior for the substrate Ala-Ala-Phe-7-amido-4-methylcoumarin (AMC) at the active site upon formalin induced amino acid cross-linking.

Original languageEnglish
Article number978668
JournalFrontiers in Chemistry
Volume10
DOIs
Publication statusPublished - Aug 31 2022

Keywords

  • amino acid modification
  • chymotrypsin
  • cross-linking
  • formalin
  • molecular docking
  • spectroscopy

ASJC Scopus subject areas

  • Chemistry(all)

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