Albert Isidro-Llobet, Mercedes Alvarez,* and Fernando Albericio* Institute for Research in Biomedicine, Barcelona Science Park, Baldiri Reixac 10, 08028 Barcelona, Spain; CIBER-BBN, Networking Centre on Bioengineering, Biomaterials and Nanomedicine, Barcelona Science Park, Baldiri Reixac 10, 08028 Barcelona, Spain; Laboratory of Organic Chemistry, Faculty of Pharmacy, University of Barcelona, 08028 Barcelona, Spain; and Department of Organic Chemistry, University of Barcelona, Marti i Franques 1, 08028 Barcelona, Spain Received April 28, 2008

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Amino Acid-Protecting Groups

Peptide therapeutics are acclaimed as a promising addition to the pharmaceutical arena, and they continue to attract interest due to their high potency, bioavailability, and fewer concerns with toxicity, drug to drug cross-reactions, and tissue accumulation. Around 700 species of marine snails of the genus Conus are distributed throughout tropical and subtropical waters. As different species preferentially hunt fish, worms, or molluscs they are categorized as piscivorous, vermivorous, or molluscivorous, respectively, although some cone snail species can feed on more than one prey type. These slow-moving creatures evolved into predators through incorporation of a specialized envenomation apparatus that enables them to quickly subdue their fast-moving prey. Conotoxins target a wide range of receptors and ion channels with unparalleled potency and selectivity. They have consequently become the subject of intense research in light of their immense diagnostic and therapeutic potential and are the focus of this review.

Discovery, synthesis, and structure-activity relationships of conotoxins.

Protecting group chemistry for the cysteine thiol group has enabled a vast array of peptide and protein chemistry over the last several decades. Increasingly sophisticated strategies for the protection, and subsequent deprotection, of cysteine have been developed, facilitating synthesis of complex disulfide-rich peptides, semisynthesis of proteins, and peptide/protein labelling in vitro and in vivo. In this review, we analyse and discuss the 60+ individual protecting groups reported for cysteine, highlighting their applications in peptide synthesis and protein science.

/pdf/cysteine-protecting-groups-applications-in-peptide-and-4h71nc3y59.pdf

Cysteine protecting groups: applications in peptide and protein science.

The S-acetamidomethyl (Acm) protecting group is widely used in the chemical synthesis of peptides that contain one or more disulfide bonds. Treatment of peptides containing S-Acm protecting group with iodine results in simultaneous removal of the sulfhydryl protecting group and disulfide formation. However, the excess iodine needs to be quenched or adsorbed as quickly as possible after completion of the disulfide bond formation in order to minimize side reactions that are often associated with the iodination step. We report a simple method for simultaneous post-cysteine (Acm) group removal quenching of iodination and isolation. Use of large volumes of diethyl ether for direct precipitation action of the oxidized peptide from the 90 or 95% aqueous acetic acid solution affords nearly quantitative recovery of largely iodine-free peptide ready for direct purification. It was successfully applied to the synthesis of various peptides including human insulin-like peptide 3 analogues. Although recovery yields were comparable to the traditionally used ascorbic acid quenching method, this new approach offers significant advantages such as more simple utility, minimal side reactions, and greater cost effectiveness.

Simultaneous Post-cysteine(S-Acm) Group Removal Quenching of Iodine and Isolation of Peptide by One Step Ether Precipitation

Thiocholine-triggered reaction in personal glucose meters for portable quantitative detection of organophosphorus pesticide.

The acetamidomethyl (Acm) group is a widely used protecting group for the thiol of cysteine during the SPPS process. We prepared the amino terminal loop of the snake alpha-neurotoxin, [Cys3,Cys23, Ser17](1-24) amide, from the linear peptide [Cys(Acm)3,23,Ser17](1-24) amide obtained by SPPS. Three different methods of deprotection of Cys(Acm) and disulfide bond formation were used: iodine, thallium(III) trifluoroacetate and mercuric acetate/potassium ferricyanide. The iodine method failed to yield the expected peptide, and gave instead the mono-iodinated tyrosine analog. The disulfide cyclized peptide obtained by thallium (III) or Hg(II) procedures displayed a MW value observed by mass spectrometry that was higher than the calculated value. The difference (MWobs-MWcalc) corresponded to a multiple of the Acm moiety, which is shifted intra- and/or intermoleculary. Furthermore, we observed, in addition to the Acm shift in the disulfide cyclized decapeptide with a highSer and Thr content (model peptide II), the dimerization phenomenon in the Tl(TFA)3 process. Therefore we conclude that a side reaction, a S--O(Ser,Thr) Acm shift, occurred during the Cys(Acm) deprotection. This shift was supported by the demonstration of Ser(O-Acm) formation in the reaction of Boc-(L)-Cys(Acm) with Tl(TFA)3 in the presence of an equimolar amount of (L)Ser. We report here the efficiency of a trivalent alcohol, glycerol, as scavenger in the both Tl(TFA)3 and mercuric/ferricyanide methods, in an attempt to circumvent this side-reaction during the disulfide bond formation step starting from a bis-Cys(Acm) peptide with a high Ser and Thr content, such as the N-terminal loop of neurotoxin, model peptide II or a similar peptide.

Side reaction during the deprotection of (S-acetamidomethyl)cysteine in a peptide with a high serine and threonine content.

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Side reaction during the deprotection of (S-acetamidomethyl)cysteine in a peptide with a high serine and threonine content.