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Fernando Albericio

Researcher at University of KwaZulu-Natal

Publications -  1012
Citations -  29912

Fernando Albericio is an academic researcher from University of KwaZulu-Natal. The author has contributed to research in topics: Peptide synthesis & Solid-phase synthesis. The author has an hindex of 76, co-authored 965 publications receiving 26146 citations. Previous affiliations of Fernando Albericio include University of Barcelona & University of Chile.

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Breaking a Couple: Disulfide Reducing Agents

TL;DR: Reducing methods for disulfide bonds are reviewed, taking into consideration the solubility of the substrates when selecting the appropriate reducing reagent.
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Synthesis and NMR structure of P41Icf, a potent inhibitor of human cathepsin L

TL;DR: P41icf behaves as a well-folded protein domain with a topology very close to the crystallographic cathepsin L-bound form, which plays a crucial role in the maturation of MHC class II molecules and antigen processing.
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“Clicking” Porphyrins to Magnetic Nanoparticles for Photodynamic Therapy

TL;DR: The results suggest that TAT-conjugated SPION-TPP nanoparticles are efficient nanodevices both for tracking drugs by means of magnetic resonance imaging (MRI)-based techniques and for treating cancer cells through photodynamic therapy, thus functioning as promising theranostic nanoagents.
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Carbosilane Dendron–Peptide Nanoconjugates as Antimicrobial Agents

TL;DR: This work synthetized first- and second-generation cationic carbosilane dendrons with a maleimide molecule on their focal point, enabling their functionalization with three different AMPs, and finds an additive effect between first-generation dendron and AMP3 whose study reveals three interesting effects.
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Preparation of de novo globular proteins based on proline dendrimers.

TL;DR: A synthetic method for the preparation of protein-like globular dendrimers derived from a combination of proline, glycine and imidazolidin ring as branching unit is described, and CD data suggest conformational plasticity of branched peptides for PPI and PPII, and a stable well-defined secondary structure of prolines for PPII.