Sudipta Ray And Dilip K. Maiti - Nanotechnology

Author Information

Sudipta Maiti is affiliated with the Department of Chemical Sciences at the Tata Institute of Fundamental Research in Mumbai, Maharashtra, India. His research primarily focuses on the interactions and behaviors of biomolecules, particularly within the context of disease-associated oligomers and lipid membranes.

Research Contributions

Sudipta Maiti's research spans various aspects of biophysics and nanotechnology, with a notable focus on the interactions between membrane phases and disease-associated oligomers. His recent work includes studies on the biophysical properties of the spike protein binding helix of human ACE2, the behavior of intrinsically disordered proteins within membranes, and the influence of serotonergic drugs on lipid bilayers. His research also explores the structural properties of amyloid oligomers and their interactions with lipid membranes, contributing significantly to our understanding of protein-membrane interactions and their implications in diseases.

Aliases

Sudipta Maiti is also known by several aliases including S Maiti, Sudip Maiti, Sudipta Ray And Dilip K. Maiti, and S. Maiti.

Publication and Citation Metrics

Metric	Value
Total Citation Count	3977
H-index	31
Total Number of Papers	166

Publications:

Coexisting Ordered and Disordered Membrane Phases Have Distinct Modes of Interaction with Disease-Associated Oligomers.

DOI: 10.1021/acs.jpcb.1c09421

Year: 2022

The vesicular membrane ‘measures’ the concentration of serotonin contained in the vesicle

DOI: 10.1016/j.bpj.2021.11.1299

Year: 2022

Do amyloid oligomers make a regular structure in the lipid membrane?

DOI: 10.1016/j.bpj.2021.11.2425

Year: 2022

Single molecule photobleaching reveals the piecewise arrangement of monomers in IAPP oligomers

DOI: 10.1117/12.2612694

Year: 2022

Serotonergic drugs modulate the phase behavior of complex lipid bilayers.

DOI: 10.1016/j.biochi.2022.04.006

Year: 2022

Membrane Insertion of Intrinsically Disordered Proteins Probed by Rotational and Triplet State Dynamics

DOI: 10.1016/J.BPJ.2020.11.1963

Year: 2021

Factors that Affect the Binding of the N-Terminal Helix of Human ACE2 to Spike Protein of SARS-CoV2

DOI: 10.1016/j.bpj.2020.11.360

Year: 2021

Rational Design of Protein-Specific Folding Modifiers.

DOI: 10.1021/jacs.1c09611

Year: 2021

Probing the Influence of Single-Site Mutations in the Central Cross-β Region of Amyloid β (1–40) Peptides

DOI: 10.3390/biom11121848

Year: 2021

Biophysical properties of the isolated spike protein binding helix of human ACE2

DOI: 10.1016/j.bpj.2021.06.017

Year: 2021

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