Enantioresolution and Binding Affinity Studies on Human Serum Albumin: Recent Applications and Trends

• Type: Another Publication in an International Scientific Journal
• Date: 2021

Authors

Teresa Cardoso (Author) ICBAS; Almeida, AS (Author) Other; Fernando Remiao (Author) FFUP; Carla Fernandes (Author) FFUP

Journal

The Journal is awaiting validation by the Administrative Services.

Title: Chemosensors

Vol. 34

Final page: 304

ISSN: 2227-9040

Indexing

ISI Web of Knowledge - 10 Citations

Scopus - 11 Citations

Other information

Authenticus ID: P-00V-PKF

DOI: 10.3390/chemosensors9110304

Abstract (EN): The interaction between proteins and drugs or other bioactive compounds has been widely explored over the past years. Several methods for analysis of this phenomenon have been developed and improved. Nowadays, increasing attention is paid to innovative methods, such as high performance affinity liquid chromatography (HPALC) and affinity capillary electrophoresis (ACE), taking into account various advantages. Moreover, the development of separation methods for the analysis and resolution of chiral drugs has been an area of ongoing interest in analytical and medicinal chemistry research. In addition to bioaffinity binding studies, both HPALC and ACE al-low one to perform other type of analyses, namely, displacement studies and enantioseparation of racemic or enantiomeric mixtures. Actually, proteins used as chiral selectors in chromatographic and electrophoretic methods have unique enantioselective properties demonstrating suitability for the enantioseparation of a large variety of chiral drugs or other bioactive compounds. This review is mainly focused in chromatographic and electrophoretic methods using human serum albumin (HSA), the most abundant plasma protein, as chiral selector for binding affinity analysis and enantioresolution of drugs. For both analytical purposes, updated examples are presented to highlight recent applications and current trends.

Language: English

Type (Professor's evaluation): Scientific

No. of pages: 34