Effect of Cosolvents on the Stabilization of Bioactive Peptides from Bovine Milk α-Casein
Peptides with more than one biological activity are many a times multifunctional peptides. Two peptides with multifunctional properties from αS2-casein were stabilized in presence of cosolvents for their biological activities like ACE inhibition activity and antioxidant activity. These bioactive peptides in cosolvents were also thermostable. Infra red spectra of peptides in cosolvents reveal no change in the secondary structure in presence of cosolvents. Correlation between sequence, structure and composition of peptides on biological activities were studied.
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Document Type: Research Article
Publication date: 2008-05-01
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- Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.