Cleavage of peptides from benzhydrylamine resins using trifluoromethanesulfonic acid

Heavner, George A.; Doyle, Donald L.; Riexinger, Douglas

doi:10.1016/s0040-4039(00)98757-4

Cited by 10 publications

(4 citation statements)

References 0 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…This solid-phase asymmetric linker (69), structurally analogous to the most successful solution phase auxiliary design, [31] was constructed starting with the benzhydrylamine (BHA) resin 68. [32] Coupling of the BHA 68 resin with both enantiomers of R-hydroxyvaline furnished the immobilized auxiliaries (S)-69 and (R)-69 (Scheme 3.18). These, in turn, were functionalized with N -acylmalonamic acid and subjected to diazotransfer, providing diazoimide resins (S)-70 and (R)-70.…”

Section: Typical Experimental Proceduresmentioning

confidence: 99%

Nucleophile Cleavable Linker Units

Porcheddu

Giacomelli

2009

Linker Strategies in Solid‐Phase Organic Synthesis

View full text Add to dashboard Cite

Section: Typical Experimental Proceduresmentioning

confidence: 99%

Nucleophile Cleavable Linker Units

Porcheddu

Giacomelli

2009

Linker Strategies in Solid‐Phase Organic Synthesis

View full text Add to dashboard Cite

“…3) were obtained by solid‐phase peptide synthesis (SPPS) using the Boc strategy with the Merrifield resin (33). Cleavage of these peptides from the resin by liquid HF (34) afforded the desired decapeptides 14 – 25 in good to moderate yields after RP‐HPLC purification.…”

Section: Chemistrymentioning

confidence: 99%

Conformational restriction of the Tyr⁵³ side‐chain in the decapeptide HEL[52‐61]: effects on binding to MHC‐II I‐A^k molecule and TCR recognition

Casimir¹,

Iterbeke²,

Nest³

et al. 2000

The Journal of Peptide Research

View full text Add to dashboard Cite

A series of conformationally restricted analogs of the hen egg lysozyme (HEL) decapeptide 52-61 in which the conformationally flexible Tyr53 residue was replaced by several more constrained tyrosine and phenylalanine analogs was prepared. Among these tyrosine and phenylalanine analogs were 1,2,3,4-tetrahydro-7-hydroxyisoquinoline-3-carboxylic acid (Htc), 1,2,3,4-tetrahydroisoquinoline-3-carboxylic acid (Tic), 4-amino- 1,2,4,5-tetrahydro-8-hydroxy-2-benzazepine-3-one (Hba), 4-amino-1,2,4,5-tetrahydro-2-benzazepine-3-one (Aba), 2-amino-6-hydroxytetralin-2-carboxylic acid (Hat) and 2-amino-5-hydroxyindan-2-carboxylic acid (Hai) in which the rotations around Calpha-Cbeta and Cbeta-Cgamma were restricted because of cyclization of the side-chain to the backbone. Synthesis of Pht-Hba-Gly-OH using a modification of the Flynn and de Laszlo procedure is described. Analogs of beta-methyltyrosine (beta-MeTyr) in which the side-chains were biased to particular side-chain torsional angles because of substitution at the beta-hydrogens were also prepared. These analogs of HEL[52-61] peptide were tested for their ability to bind to the major histocompatibility complex class II I-Ak molecule and to be recognized in this context by two T-cell hybridomas, specific for the parent peptide HEL[52-61]. The data showed that the conformation and also the configuration of the Tyr53 residue influenced both the binding of the peptide to I-Ak and the recognition of the peptide/I-Ak complex by a T-cell receptor.

show abstract

“…This migration is specially known as a side reaction of Ser-or Thr-containing peptides [5][6][7][8][9]. -Hydroxyl groups are acylated in -hydroxy--amino acids by the N-O shift under strong acidic conditions through a five-membered ring intermediate, [10][11][12][13][14][15][16][17][18]. The opposite rearrangement has also been reported [19][20][21][22] and named as an O-N intramolecular acyl migration reaction as well as an acyl shift or acyl transfer reaction (Fig.…”

Section: Introductionmentioning

confidence: 99%

Application of the O-N Intramolecular Acyl Migration Reaction in Medicinal Chemistry

Skwarczynski¹,

Kiso

2007

CMC

View full text Add to dashboard Cite

The O-N intramolecular acyl migration, also named as an acyl shift or acyl transfer reaction, is well-known in organic and peptide chemistry as a simple rearrangement which proceeds under very mild aqueous conditions. Despite a long history with this reaction, its application in medicinal chemistry has only lately been proposed. In the last decade, this reaction has been intensively studied and several applications of this rearrangement in medicinal chemistry have appeared. O-N Intramolecular acyl migration has been employed in "no auxiliary, no byproduct" prodrug strategies (prodrugs of paclitaxel and other taxoids, prodrugs of HIV protease inhibitors), for the synthesis of peptides containing difficult sequences via "O-acyl isopeptide method", including Alzheimer's disease related amyloid beta peptide (Abeta) 1-42, and in the design of pH-, photo- or enzyme-triggered click peptides, as a potential powerful tool for identifying the pathological functions of amyloid beta peptides in Alzheimer's disease. This review summarized recent advances in the application of O-N intramolecular acyl migration with special focus on medicinal chemistry.

show abstract

Cleavage of peptides from benzhydrylamine resins using trifluoromethanesulfonic acid

Cited by 10 publications

References 0 publications

Nucleophile Cleavable Linker Units

Nucleophile Cleavable Linker Units

Conformational restriction of the Tyr⁵³ side‐chain in the decapeptide HEL[52‐61]: effects on binding to MHC‐II I‐A^k molecule and TCR recognition

Application of the O-N Intramolecular Acyl Migration Reaction in Medicinal Chemistry

Contact Info

Product

Resources

About

Cleavage of peptides from benzhydrylamine resins using trifluoromethanesulfonic acid

Cited by 10 publications

References 0 publications

Nucleophile Cleavable Linker Units

Nucleophile Cleavable Linker Units

Conformational restriction of the Tyr53 side‐chain in the decapeptide HEL[52‐61]: effects on binding to MHC‐II I‐Ak molecule and TCR recognition

Application of the O-N Intramolecular Acyl Migration Reaction in Medicinal Chemistry

Contact Info

Product

Resources

About

Conformational restriction of the Tyr⁵³ side‐chain in the decapeptide HEL[52‐61]: effects on binding to MHC‐II I‐A^k molecule and TCR recognition