caa a22 4500 605511772 CHVBK 20210128100652.0 cr unu---uuuuu 210128e20151201xx s 000 0 eng 10.1007/s00894-015-2847-2 doi (NATIONALLICENCE)springer-10.1007/s00894-015-2847-2 An investigation of folic acid-protein association sites and the effect of this association on folic acid self-assembly [Elektronische Daten] [Rajat Gupta, Prasanta Kalita, Omkar Patil, Sanat Mohanty] The contribution of folic acid (FA)-tryptophan interactions to FA-protein association was investigated in the context of using FA as a drug carrier in protein delivery systems. Bovine serum albumin (BSA) and indolicidin were used as model proteins in the study. The FA-BSA complex was characterized by using the Bradford reagent to identify the impact of FA-BSA association on BSA-dye reagent interactions. UV-visible spectroscopic analysis of the FA-BSA mixture showed that the absorbance maximum of BSA-dye reagent occurred at 595nm, even after the association of FA with BSA. This confirms that protonated amino acid groups of the protein are not involved in FA-BSA association. Moreover, molecular dynamics (MD) simulation confirmed the presence of an associative interaction between aromatic moieties in FA and tryptophan moieties in the indolicidin molecule, which disrupted FA self-assembly. An X-ray diffraction (XRD) study showed that there was limited disruption of FA self-assembly after the addition of BSA or tryptophan. This suggests that FA and BSA are compatible and associate with each other. Graphical Abstract Mechanism of folic acid and protein association Springer-Verlag Berlin Heidelberg, 2015 Folate nationallicence Tryptophan nationallicence Molecular dynamics nationallicence Indolicidin nationallicence Spectroscopy nationallicence Gupta Rajat Department of Chemical Engineering, Indian Institute of Technology Delhi, 110016, New Delhi, India aut Kalita Prasanta Department of Chemical Engineering, Indian Institute of Technology Delhi, 110016, New Delhi, India aut Patil Omkar Department of Chemical Engineering, Indian Institute of Technology Delhi, 110016, New Delhi, India aut Mohanty Sanat Department of Chemical Engineering, Indian Institute of Technology Delhi, 110016, New Delhi, India aut Journal of Molecular Modeling Springer Berlin Heidelberg 21/12(2015-12-01), 1-8 1610-2940 21:12<1 2015 21 894 https://doi.org/10.1007/s00894-015-2847-2 text/html Onlinezugriff via DOI BK010053 XK010053 XK010000 Metadata rights reserved Springer special CC-BY-NC licence nationallicence 1 research-article jats NATIONALLICENCE NATIONALLICENCE NL-springer NATIONALLICENCE 856 40 https://doi.org/10.1007/s00894-015-2847-2 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Gupta Rajat Department of Chemical Engineering, Indian Institute of Technology Delhi, 110016, New Delhi, India aut NATIONALLICENCE 700 1- Kalita Prasanta Department of Chemical Engineering, Indian Institute of Technology Delhi, 110016, New Delhi, India aut NATIONALLICENCE 700 1- Patil Omkar Department of Chemical Engineering, Indian Institute of Technology Delhi, 110016, New Delhi, India aut NATIONALLICENCE 700 1- Mohanty Sanat Department of Chemical Engineering, Indian Institute of Technology Delhi, 110016, New Delhi, India aut NATIONALLICENCE 773 0- Journal of Molecular Modeling Springer Berlin Heidelberg 21/12(2015-12-01), 1-8 1610-2940 21:12<1 2015 21 894