Identification and prioritization of potential therapeutic molecules against LpxA from - A computational study.

A. baumannii is a ubiquitously found gram-negative, multi-drug resistant bacterial species from the ESKAPE family of pathogens known to be the causative agent for hospital-acquired infections such as pneumonia, meningitis, endocarditis, septicaemia and urinary tract infections. is implicated as a contributor to bloodstream infections in approximately 2% of all worldwide infections.

Structural evidence of the oxidation of iodide ion into hyper-reactive hypoiodite ion by mammalian heme lactoperoxidase.

Lactoperoxidase (1.11.1.

Identifying the natural compound Catechin from tropical mangrove plants as a potential lead candidate against 3CL from SARS-CoV-2: An integrated approach.

SARS-CoV-2, a member of beta coronaviruses, is a single-stranded, positive-sense RNA virus responsible for the COVID-19 pandemic. With global fatalities of the pandemic exceeding 4.57 million, it becomes crucial to identify effective therapeutics against the virus.

A comprehensive review on promising anti-viral therapeutic candidates identified against main protease from SARS-CoV-2 through various computational methods.

Background: The COVID-19 pandemic caused by SARS-CoV-2 has shown an exponential trend of infected people across the planet. Crediting its virulent nature, it becomes imperative to identify potential therapeutic agents against the deadly virus. The 3-chymotrypsin-like protease (3CLpro) is a cysteine protease which causes the proteolysis of the replicase polyproteins to generate functional proteins, which is a crucial step for viral replication and infection.

Identification of promising antiviral drug candidates against non-structural protein 15 (NSP15) from SARS-CoV-2: an assisted drug-repurposing study.

The recent COVID-19 pandemic caused by SARS-CoV-2 has recorded a high number of infected people across the globe. The virulent nature of the virus makes it necessary for us to identify promising therapeutic agents in a time-sensitive manner. The current study utilises an based drug repurposing approach to identify potential anti-viral drug candidates targeting non-structural protein 15 (NSP15), i.

A Comprehensive In Silico Study Towards Understanding the Inhibitory Mechanism of Lactoperoxidase by Dapsone and Propofol.

Introduction: Lactoperoxidase (LPO) is a member of the mammalian heme peroxidase family and is an enzyme of the innate immune system. It possesses a covalently linked heme prosthetic group (a derivative of protoporphyrin IX) in its active site. LPO catalyzes the oxidation of halides and pseudohalides in the presence of hydrogen peroxide (HO) and shows a broad range of the antimicrobial activity.

Diabetes in Appalachia: providers' perspectives.

Background: Southeastern Appalachian Ohio has more than double the national average of diabetes and a critical shortage of healthcare providers. Paradoxically, there is limited research focused on primary care providers' experiences treating people with diabetes in this region. This study explored providers' perceived barriers to and facilitators for treating patients with diabetes in southeastern Appalachian Ohio.

Targeting SARS-CoV-2: a systematic drug repurposing approach to identify promising inhibitors against 3C-like proteinase and 2'-O-ribose methyltransferase.

The recent pandemic associated with SARS-CoV-2, a virus of the Coronaviridae family, has resulted in an unprecedented number of infected people. The highly contagious nature of this virus makes it imperative for us to identify promising inhibitors from pre-existing antiviral drugs. Two druggable targets, namely 3C-like proteinase (3CLpro) and 2'-O-ribose methyltransferase (2'-O-MTase) were selected in this study due to their indispensable nature in the viral life cycle.

Dual binding mode of antithyroid drug methimazole to mammalian heme peroxidases - structural determination of the lactoperoxidase-methimazole complex at 1.97 Å resolution.

Lactoperoxidase (LPO, EC 1.11.1.

Lactoperoxidase: structural insights into the function,ligand binding and inhibition.

Lactoperoxidase (LPO) is a member of a large group of mammalian heme peroxidases that include myeloperoxidase (MPO), eosinophil peroxidase (EPO) and thyroid peroxidase (TPO). The LPO is found in exocrine secretions including milk. It is responsible for the inactivation of a wide range of micro-organisms and hence, is an important component of defense mechanism in the body.