G
Gopinath Kasetty
Researcher at Lund University
Publications - 35
Citations - 956
Gopinath Kasetty is an academic researcher from Lund University. The author has contributed to research in topics: Antimicrobial & Antimicrobial peptides. The author has an hindex of 15, co-authored 34 publications receiving 824 citations. Previous affiliations of Gopinath Kasetty include University of Gothenburg.
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Journal ArticleDOI
Chemerin Is an Antimicrobial Agent in Human Epidermis
Magdalena Banas,Katarzyna Zabieglo,Gopinath Kasetty,Monika Kapinska-Mrowiecka,Julia Borowczyk,Justyna Drukala,Krzysztof Murzyn,Brian A. Zabel,Eugene C. Butcher,Jens M. Schroeder,Artur Schmidtchen,Joanna Cichy +11 more
TL;DR: It is demonstrated that endogenous chemerin is abundant in human epidermis, and that inhibition of bacteria growth by exudates from organ cultures of primary human skin keratinocytes is largely cheMERin-dependent.
Journal ArticleDOI
Highly selective end-tagged antimicrobial peptides derived from PRELP.
TL;DR: Hydrophobic C-terminal end-tagging of the cationic sequence RRPRPRPRP generates highly selective AMPs with potent activity against multiresistant bacteria and efficiency in ex vivo wound infection models.
Journal ArticleDOI
Membrane selectivity by W-tagging of antimicrobial peptides.
Artur Schmidtchen,Lovisa Ringstad,Gopinath Kasetty,Hiroyasu Mizuno,Mark W. Rutland,Martin Malmsten +5 more
TL;DR: The generality of the high membrane selectivity for other peptides of this type is demonstrated, andReplacing cholesterol with ergosterol results in an increased sensitivity for peptide-induced lysis, in analogy to the antifungal properties of such peptides.
Journal ArticleDOI
Antimicrobial activity of fibrinogen and fibrinogen-derived peptides--a novel link between coagulation and innate immunity
Lisa I. Påhlman,Matthias Mörgelin,Gopinath Kasetty,Anders I. Olin,Artur Schmidtchen,Heiko Herwald +5 more
TL;DR: It is shown that the viability of fibrinogen-binding bacteria is affected in human plasma activated with thrombin, and it is found that the peptide fragment GHR28 released from the β-chain of fibinogen has antimicrobial activity against bacteria that bind fibr inogen to their surface, whereas non-binding strains are unaffected.
Journal ArticleDOI
C-terminal Peptides of Tissue Factor Pathway Inhibitor Are Novel Host Defense Molecules
Praveen Papareddy,Martina Kalle,Gopinath Kasetty,Matthias Mörgelin,Victoria Rydengård,Barbara Albiger,Katarina Lundqvist,Martin Malmsten,Artur Schmidtchen +8 more
TL;DR: C-terminal TFPI peptide sequences are antimicrobial against the Gram-negative bacteria Escherichia coli and Pseudomonas aeruginosa, Gram-positive Bacillus subtilis and Staphylococcus aureus, as well as the fungi Candida albicans and Candida parapsilosis.