Summary Human Serum albumin (HSA) is a plasma protein in charge of the transportation of the fatty acids (Bhattacharya, Grune & Curry, 2000, p.721). HSA promotes the transportation capacity of plasma because it is currently at around 0.6Mm enabling it to carry more than six molecules of fatty acid. In addition, the HSA binds and agitates the pharmacokinetics of various drugs compounds. The HSA-fatty acid has two drug-binding sites, which are the sub-domains IIA and IIIA. The fatty acid IIIA coincides with the high affinity of the long-chain fatty acid binding site. One of the features of the HSA is that it is capable of binding a variety of drugs. Most of the clinical and pharmaceutical interest in the protein is derived from the impacts
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The structure of the HSA –fatty acid allows an extensive interaction of the medium and long-chain fatty acid protein. In the HAS-fatty acid, there is a chain length of ten to 18 carbon atoms to accommodate the different lengths of the fatty acid. Moreover, the binding sites are distributed in three homologous domains of the HSA through which each domain accommodates the fatty acids in different ways. The structure of the HSA facilitates the binding of the fatty acid to the albumin setting up a dependable map of the fatty acid binding location. The structure of the HSA facilitates direct approaches such as mutagenesis and high resolution of the NMR. The structure of the fatty acids facilitates their widespread in the circulation resulting to the binding of site II drugs, which are vulnerable to variations in the plasma levels of fatty acid or …show more content…
In site 1, the electron density is for the medium chain fatty acids although in their respective complexes the density is weaker and broken for the longer fatty acids. The location of site 2 is between the sub-domains IA and IIA. Site 2 is made of the fatty acid binding sites on HAS. In this site, the carboxylate moiety of the ligand is shielded from solvent. The density at this is conducive for all the fatty acids. Site 3 and 4 contain two molecules of C14:0. The molecules are bind at right angles with their methylene tails in contact. However, site 4 is longer and narrower than site 3. A site 6 bases the fragmentary density of the original analysis of HAS-C14:0 complexes identified as the sixth fatty acid binding site in between sub –domain IIA and IIB. The fatty acids modeled at this site are built with their carboxylate group interacting with IIB. Site 7 is considerable small .In this site the fatty acids bind in a curved configuration while the tail is co-planar with aromatic drugs that bind at this site. Site 9 and 10 are located in the inter-domain crevice with site 9 having an open binding environment, which faces the bottom of the crevice to be in contact with the protein. Both ends have the binding pocket with the distributions of the polar side chains that shape the electron density excluding the possibility of the orientation of the
The structure of the HSA –fatty acid allows an extensive interaction of the medium and long-chain fatty acid protein. In the HAS-fatty acid, there is a chain length of ten to 18 carbon atoms to accommodate the different lengths of the fatty acid. Moreover, the binding sites are distributed in three homologous domains of the HSA through which each domain accommodates the fatty acids in different ways. The structure of the HSA facilitates the binding of the fatty acid to the albumin setting up a dependable map of the fatty acid binding location. The structure of the HSA facilitates direct approaches such as mutagenesis and high resolution of the NMR. The structure of the fatty acids facilitates their widespread in the circulation resulting to the binding of site II drugs, which are vulnerable to variations in the plasma levels of fatty acid or …show more content…
In site 1, the electron density is for the medium chain fatty acids although in their respective complexes the density is weaker and broken for the longer fatty acids. The location of site 2 is between the sub-domains IA and IIA. Site 2 is made of the fatty acid binding sites on HAS. In this site, the carboxylate moiety of the ligand is shielded from solvent. The density at this is conducive for all the fatty acids. Site 3 and 4 contain two molecules of C14:0. The molecules are bind at right angles with their methylene tails in contact. However, site 4 is longer and narrower than site 3. A site 6 bases the fragmentary density of the original analysis of HAS-C14:0 complexes identified as the sixth fatty acid binding site in between sub –domain IIA and IIB. The fatty acids modeled at this site are built with their carboxylate group interacting with IIB. Site 7 is considerable small .In this site the fatty acids bind in a curved configuration while the tail is co-planar with aromatic drugs that bind at this site. Site 9 and 10 are located in the inter-domain crevice with site 9 having an open binding environment, which faces the bottom of the crevice to be in contact with the protein. Both ends have the binding pocket with the distributions of the polar side chains that shape the electron density excluding the possibility of the orientation of the