F
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.
Papers
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Journal Article
Functionalized resins and linkers for solid-phase synthesis of small molecules
Journal ArticleDOI
Successful development of a method for the incorporation of Fmoc-Arg(Pbf)-OH in solid-phase peptide synthesis using N-butylpyrrolidinone (NBP) as solvent
Beatriz G. de la Torre,Ashok Kumar,Mahama Alhassan,Christoph Bucher,Fernando Albericio,Fernando Albericio,John Lopez +6 more
TL;DR: In this paper, the authors studied the incorporation of Fmoc-Arg(Pbf)-OH, one of the most problematic amino acids, into a growing peptide chain.
Book ChapterDOI
Poly(ethylene glycol)-containing supports for solid-phase synthesis of peptides and combinatorial organic libraries.
TL;DR: This chapter reviews the preparation of families of poly(ethylene glycol)-polystyrene (PEG-PS)graft as well as Cross-Linked Ethoxylate Acrylate Resin (CLEAR) supports developed in the authors' laboratories, and demonstrates their applications to the syntheses of a wide range of targets in connection with numerous research objectives.
Journal ArticleDOI
Facile solid-phase synthesis of biotinylated alkyl thiols
Elisabet Prats-Alfonso,Fayna Garcia-Martin,Nuria Bayó,Luis J. Cruz,Mateu Pla-Roca,Josep Samitier,Abdelhamid Errachid,Fernando Albericio +7 more
TL;DR: 2-Chlorotrityl Chloride solid-phase resin is proposed as a new platform to produce functionalized alkyl thiols with the capacity to graft avidin proteins for self-assembled monolayers on gold.
Journal ArticleDOI
Tetrahydropyranyl, a nonaromatic acid-labile Cys protecting group for Fmoc peptide chemistry.
TL;DR: Tetrahydropyranyl (Thp), which exploits the concept of being an S,O-acetal nonaromatic protecting group for cysteine, has been shown to be superior to Trt, Dpm, Acm, and StBu in solid-phase peptide synthesis using the Fmoc/tBu strategy.