Publications by authors named "Bishal Gautam"

Superior vena cava (SVC) flow has been considered a surrogate marker of systemic blood flow in neonates. We conducted a systematic review to evaluate the association between low SVC flow recorded during the early neonatal period and neonatal outcomes. We searched the following databases (until December 9, 2020; updated October 21, 2022): PROSPERO, OVID Medline, OVID EMBASE, Cochrane Library (CDSR and Central), Proquest Dissertations and Theses Global, and SCOPUS using controlled vocabulary and key words representing the concepts "superior vena cava" and "flow" and "neonate.

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The interactions of proteins with surfaces are important in both biological processes and biotechnologies. In contrast to decades of study regarding the biophysics of proteins in bulk solution, however, our mechanistic understanding of the biophysics of proteins interacting with surfaces remains largely qualitative. In response, we have set to explore quantitatively the thermodynamics of protein-surface interactions.

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Plasma-derived polyclonal antibody therapeutics, such as intravenous immunoglobulin, have multiple drawbacks, including low potency, impurities, insufficient supply and batch-to-batch variation. Here we describe a microfluidics and molecular genomics strategy for capturing diverse mammalian antibody repertoires to create recombinant multivalent hyperimmune globulins. Our method generates of diverse mixtures of thousands of recombinant antibodies, enriched for specificity and activity against therapeutic targets.

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Objective: Laryngeal mask airway (LMA) has emerged as an alternative surfactant delivery method. The effectiveness of this method for the delivery of surfactant is uncertain. A meta-analysis of randomized control trials (RCTs) comparing LMA with standard methods of surfactant delivery for the outcomes of surfactant dose repetition, oxygen requirement, mechanical ventilation, intubation, mortality, bronchopulmonary dysplasia (BPD), and pneumothorax.

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The physics of proteins interacting with surfaces can differ significantly from those seen when the same proteins are free in bulk solution. As an example, we describe here the extent to which site-specific attachment to a chemically well-defined macroscopic surface alters the ability of several stabilizing and destabilizing cosolutes to modulate protein folding thermodynamics. We determined this via guanidinium denaturations performed in the presence of varying concentrations of cosolutes when proteins were either site-specifically attached to self-assembled monolayers on gold or free in bulk solution.

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