ArticleAmino acids2022
Far-UV circular dichroism signatures indicate fluorophore labeling induced conformational changes of penetratin.
Article in Amino acids, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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Who cites it
2 citing papers in PubMed, 6 citations in OpenAlex.
- GPepT: A Foundation Language Model for Peptidomimetics Incorporating Noncanonical Amino Acids.ACS medicinal chemistry letters · 2025Article
- Evaluation of Methods Employed in Establishing Preclinical Similarity of Adalimumab Biosimilars.Advances in pharmacological and pharmaceutical sciences · 2025Review
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1 author at 1 institution in 1 country.
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Abstract
Fluorescent labeling is a broadly utilized approach to assess in vitro and in vivo behavior of biologically active, especially cell-penetrating and antimicrobial peptides. In this communication, far-UV circular dichroism (CD) spectra of penetratin (PEN) fluorophore conjugates reported previously have been re-evaluated. Compared to the intrinsically disordered native peptide, rhodamine B and carboxyfluorescein derivatives of free and membrane-bound PEN exhibit extrinsic CD features. Potential sources of these signals displayed above 220 nm are discussed suggesting the contributions of both intra- and intermolecular chiral exciton coupling mechanisms. Careful evaluation of the CD spectra of fluorophore-labeled peptides is a valuable tool for early detection of labeling-provoked structural alterations which in turn may modify the membrane binding and cellular uptake compared to the unconjugated form.
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