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Trypsin inhibitor complexes with human and bovine serum albumins: TEM and spectroscopic analysis

Paper ID Volume ID Publish Year Pages File Format Full-Text
30444 44478 2014 6 PDF Available
Title
Trypsin inhibitor complexes with human and bovine serum albumins: TEM and spectroscopic analysis
Abstract

•Trypsin inhibitor (TI) binds HSA and BSA via hydrophilic and hydrophobic contacts.•BSA forms more stable complexes than HSA.•Trypsin inhibitor complexation alters protein secondary structure.•TEM shows serum protein aggregation and fibrillation upon TI interaction.

We report the binding of trypsin inhibitor (TI) with human serum albumin (HSA) and bovine serum albumin (BSA) at physiological conditions, using FTIR, CD, UV–Visible spectroscopic methods and transmission electron microscopy (TEM). Structural analysis showed that trypsin inhibitor binds HSA and BSA via hydrophilic and hydrophobic contacts with overall binding constants of KTI-HSA = 1.4 (±0.5) × 104 M−1 and KTI-BSA = 1.1 (±0.4) × 106 M−1. Trypsin inhibitor complexation induces minor reduction of the protein α-helix and a major increase in β-sheet structure. TEM images show that trypsin inhibitor complex formation leads to the protein aggregation and fibrillation.

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Keywords
Trypsin inhibitor; Serum albumin; Binding site; Spectroscopy; TEM images
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Publisher
Database: Elsevier - ScienceDirect
Journal: Journal of Photochemistry and Photobiology B: Biology - Volume 130, 5 January 2014, Pages 254–259
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
100% Money Back Guarantee
Full-text PDF Download
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Any Questions? feel free to contact us