{"id":5312,"date":"2026-05-18T12:31:05","date_gmt":"2026-05-18T12:31:05","guid":{"rendered":"https:\/\/cognitionconferences.com\/hivaids\/?post_type=speaker&p=5312"},"modified":"2026-05-18T12:36:54","modified_gmt":"2026-05-18T12:36:54","slug":"komal-hayat","status":"publish","type":"speaker","link":"https:\/\/cognitionconferences.com\/hivaids\/speaker\/komal-hayat\/","title":{"rendered":"Komal Hayat"},"content":{"rendered":"

Abstract :
\n<\/strong>
\nHuman immunodeficiency virus type 1 (HIV-1) remains a major global health challenge, sustaining the need for structurally improved protease inhibitors with enhanced potency, bioavailability, and resistance profiles. This work reports the design and synthesis of a phosphinic lopinavir analogue, PL1, in which the hydroxyethylene core of lopinavir was replaced with a phosphinic acid functionality. This modification was intended to strengthen interactions with the catalytic site of HIV-1 protease and provide a distinct transition-state-mimicking pseudopeptidic scaffold. Enzymatic evaluation demonstrated promising inhibitory activity of PL1 against HIV-1 protease, while molecular dynamics simulations supported its favorable binding stability and key active-site interactions.<\/p>\n

The work further establishes an efficient synthetic strategy to access diverse symmetrical phosphinic acid scaffolds designed according to HIV-1 protease enzyme\u2013substrate specificity. Several compounds exhibited strong inhibitory activity, with IC\u2085\u2080 values in the low nanomolar range. Diastereomeric resolution of the most active compound identified a highly potent isomer with an IC\u2085\u2080 value of 1 nM. Molecular docking analysis revealed favorable binding orientations stabilized by strong hydrogen-bonding interactions with critical residues in the protease active site.<\/p>\n

To address the inherent absorption limitations commonly associated with phosphinic acid-based drug candidates, a mild and efficient esterification protocol was developed specifically for the symmetrical phosphinic acid scaffold. The method enabled derivatization of the phosphinic acid moiety with carbohydrate and flavonoid promoieties in excellent to quantitative yields using highly effective peptide-coupling reagents, including TBTU and DIC. These ester derivatives represent potential prodrug candidates with anticipated low toxicity and the capacity to generate naturally occurring carbohydrate metabolites or flavonoid fragments associated with hepatoprotective effects.<\/p>\n

Collectively, these findings highlight phosphinic pseudopeptides as promising scaffolds for HIV-1 protease inhibitors and provide a synthetic platform for future pharmacokinetic optimization and prodrug development.<\/p>\n

Biography:<\/strong><\/p>\n

Komal Hayat completed her PhD in Chemistry at the University of Liverpool, through a fully funded studentship at Xi\u2019an Jiaotong-Liverpool University (campus). Her research focused on organic synthesis, asymmetric catalysis, and medicinal chemistry, particularly the development of architecturally complex molecules and phosphinic-based HIV inhibitors. She has worked as a Lecturer in Chemistry, Research Assistant at Quaid-i-Azam University, and Teaching Assistant at Xi\u2019an Jiaotong-Liverpool University. She has published 10 research articles in reputed journals, including Bioorganic Chemistry and ACS Omega, and has presented her work at international scientific conferences.<\/p>\n","protected":false},"featured_media":5315,"template":"","meta":{"_acf_changed":false},"schedule":[7],"speaker-category":[6],"class_list":["post-5312","speaker","type-speaker","status-publish","has-post-thumbnail","hentry","schedule-day-2","speaker-category-speakers"],"acf":[],"yoast_head":"\nKomal Hayat | Xi\u2019an Jiaotong Liverpool University | China<\/title>\n<meta name=\"description\" content=\"Komal Hayat completed her PhD in Chemistry at the University of Liverpool, through a fully funded studentship at Xi\u2019an Jiaotong-Liverpool University (campus). Her research focused on organic synthesis, asymmetric catalysis, and medicinal chemistry, particularly the development of architecturally complex molecules and phosphinic-based HIV inhibitors. 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