Interactions of tuftsin with bovine serum albumin

FEBS Letters
V Bhakuni, C M Gupta

Abstract

Interactions of tuftsin (Thr-Lys-Pro-Arg) with bovine serum albumin (BSA) were analysed by fluorescence spectroscopy and circular dichroism. The data show that tuftsin interacts weakly with BSA, but this interaction is considerably enhanced by introducing an apolar substituent at the C-terminus of the tetrapeptide. It is suggested that strong binding of tuftsin to albumin in blood may enhance its macrophage-stimulating activity in vivo.

References

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Citations

Jul 7, 1987·Biochimica Et Biophysica Acta·H W Dirr, J C Schabort
Sep 1, 2000·Advanced Drug Delivery Reviews·S P Vyas, V Sihorkar
Mar 4, 2000·Advanced Drug Delivery Reviews·A K Agrawal, C M Gupta
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Sep 2, 2006·Chemical & Pharmaceutical Bulletin·Hedong BianHong Liang
Apr 1, 2008·Spectrochimica Acta. Part A, Molecular and Biomolecular Spectroscopy·Hui XuYanqing Wen
Apr 10, 2007·Spectrochimica Acta. Part A, Molecular and Biomolecular Spectroscopy·Xiuying ZhangChangqing Fan
May 30, 2006·International Journal of Biological Macromolecules·Hedong BianHong Liang
Dec 21, 2020·Advances in Colloid and Interface Science·Joëlle Bizeau, Damien Mertz

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