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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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Journal ArticleDOI

3-(1-Piperidinyl)alanine formation during the preparation ofC-terminal cysteine peptides with the Fmoc/t-Bu strategy

TL;DR: MALDI-TOF analysis was a useful analytical technique to determine the phenomenon of base-catalyzed elimination of the sulfhydryl-protected side-chain to afford the dehydroalanine derivative followed by a nucleophilic addition to the alkene.
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The effect of N-methylation of amino acids (Ac-X-OMe) on solubility and conformation: a DFT study

TL;DR: The results reveal that after mono N-methylation of the peptide backbone, ΔGsolv becomes more negative (more water soluble) while polarizability and dipole moment are also increased, and natural atomic charges derived by natural bond orbital (NBO) analysis of N, C, and O atoms involved in amide functional group become more positive/(less negative) after N- methylation.
Book ChapterDOI

Convergent solid-phase peptide synthesis.

TL;DR: Convergent solid-phase peptide synthesis (CSPPS) involves solidphase synthesis of protected peptides (these must retain the protecting groups of the N α -amino and the side-chain functions after cleavage from the resin), purification and characterization of the protected peptide segments, and their solid- phase coupling.
Journal ArticleDOI

RNA binding characteristics of a 16 kDa glycine-rich protein from maize.

TL;DR: It is shown that the MA16-encoded protein binds preferentially to uridine- and guanosine-rich RNAs, suggesting a likely role for this protein in RNA metabolism during late embryogenesis and in the stress response.
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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.