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Lorena Mendive-Tapia

Researcher at University of Edinburgh

Publications -  30
Citations -  831

Lorena Mendive-Tapia is an academic researcher from University of Edinburgh. The author has contributed to research in topics: Medicine & Peptide. The author has an hindex of 11, co-authored 20 publications receiving 521 citations. Previous affiliations of Lorena Mendive-Tapia include University of KwaZulu-Natal & Park University.

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New peptide architectures through C–H activation stapling between tryptophan–phenylalanine/tyrosine residues

TL;DR: A synthetic strategy for the preparation of unique constrained peptides featuring a covalent bond between tryptophan and phenylalanine or tyrosine residues through an intramolecular palladium-catalysed C–H activation process is described.
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Synthesis of C-2 Arylated Tryptophan Amino Acids and Related Compounds through Palladium-Catalyzed C–H Activation

TL;DR: A C-H activation process allows the preparation of both protected and unprotected arylated-Trp amino acids, directly from the amino acid precursor and aryl iodides, suitable for standard solid-phase peptide synthesis.
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Spacer-free BODIPY fluorogens in antimicrobial peptides for direct imaging of fungal infection in human tissue

TL;DR: A fluorogenic probe to image Aspergillus fumigatus directly in human pulmonary tissue and a fluorogenic Trp-BODIPY amino acid with a spacer-free C-C linkage between Trp and a BODIPy fluorogen, which shows remarkable fluorescence enhancement in hydrophobic microenvironments are reported.
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Constrained Cyclopeptides: Biaryl Formation through Pd-Catalyzed C-H Activation in Peptides-Structural Control of the Cyclization vs. Cyclodimerization Outcome.

TL;DR: A series of short tryptophan-phenylalanine peptides containing an iodo substituent on the phenyl ring was subjected to Pd-catalyzed CH activation reactions to give the corresponding aryl-indole coupled products.
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A Trp-BODIPY cyclic peptide for fluorescence labelling of apoptotic bodies

TL;DR: Affinity assays, confocal microscopy and flow cytometry analysis confirmed the binding of the peptide to negatively-charged phospholipids associated with apoptosis, and its applicability for the detection and characterisation of subcellular structures released by apoptotic cells.