Application of AM SURE™ resin to solid-phase peptide synthesis

Lee, Taekyung; Lee, Sang-Myung; Ryoo, Sun-Jong; Byun, Jang‐Woong; Lee, Yoon‐Sik

doi:10.1016/j.tetlet.2005.08.093

Cited by 14 publications

(10 citation statements)

References 11 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Lee and co‐workers also demonstrated a highly successful synthesis of the “difficult peptide,” ACP 65‐74 , using the AminoMethyl SUrface‐layered polystyrene REsin (AM‐ SURE ) resin (Lee et al, ). AM‐ SURE is a 1% divinylbenzene (DVB) cross‐linked polystyrene resin (BeadTech), which is a nonpolar support but which has the functionalized linker groups located on the surface of each resin bead.…”

Section: Aids In the Synthesis Of “Difficult Peptide” Sequencesmentioning

confidence: 99%

Overview of Solid Phase Synthesis of “Difficult Peptide” Sequences

Tickler

Wade

2007

CP Protein Science

View full text Add to dashboard Cite

Solid-phase peptide synthesis has contributed immeasurably to the understanding of the chemistry and biology of peptides by enabling their ready preparation in small quantities up to the ton scale. The advantages of the technology, including its simplicity, ease of operation, and general efficiency have far outweighed its limitations. However, despite the general effectiveness of the solid phase synthesis methodology, some peptides are resistant to efficient assembly and are known as "difficult peptides." Such sequences can present serious challenges to the peptide researcher and have been the subject of considerable investigation. This phenomenon is described together with modern approaches designed to minimize or overcome this hitherto long-standing and vexing problem.

show abstract

Section: Aids In the Synthesis Of “Difficult Peptide” Sequencesmentioning

confidence: 99%

Overview of Solid Phase Synthesis of “Difficult Peptide” Sequences

Tickler

Wade

2007

CP Protein Science

View full text Add to dashboard Cite

show abstract

“…Given the above results, we were interested to see whether the performance of the coupling reagents was peptide‐dependent. Thus, we selected the Jung–Redemann 10‐mer (WFTTLISTIM‐NH 2 ) as another difficult model sequence . After initial methionine coupling with a coupling yield of >99.8%, the decapeptide was assembled on the SCAL‐G 3 ‐AM ChemMatrix® resin employing HBTU, HCTU, or COMU and applying the 4.3‐minute coupling cycle (three‐minute pre‐activation/one‐minute coupling) (Figure and Table ).…”

Section: Resultsmentioning

confidence: 99%

Evaluation of COMU as a coupling reagent for in situ neutralization Boc solid phase peptide synthesis

Hjørringgaard

Brust

Alewood

2012

Journal of Peptide Science

View full text Add to dashboard Cite

Benzotriazole‐based coupling reagents have dominated the last two decades of solid phase peptide synthesis. However, a growing interest in synthesizing complex peptides has stimulated the search for more efficient and low‐cost coupling reagents, such as COMU which has been introduced as a nonexplosive alternative to the classic benzotriazole coupling reagents. Here, we present a comparative study of the coupling efficiency of COMU with the benzotriazole‐based HBTU and HCTU for use in in situ neutralization Boc‐SPPS. Difficult sequences, such as ACP(65–74), Jung–Redeman 10‐mer, and HIV‐1 PR(81–99), were used as model target peptides on polystyrene‐based resins, as well as polyethylene glycol‐based resins. Coupling yields obtained using fast in situ Boc‐SPPS cycles were determined with the quantitative ninhydrin test as well as via LC‐MS analysis of the crude cleavage products. Our results demonstrate that COMU coupling efficiency was less effective compared to HBTU and HCTU with HCTU ≥ HBTU > COMU, when polystyrene‐based resins were employed. However, when the PEG resin was employed in combination with a safety catch amide (SCAL) linker, more comparable yields were observed for the three coupling reagents with the same ranking HCTU ≥ HBTU > COMU. Copyright © 2012 European Peptide Society and John Wiley & Sons, Ltd.

show abstract

“…The peptide sequences of Fmoc‐Ile‐Thr‐P 2 ‐Arg‐Gly‐Phe‐Ala‐NH 2 (P 2 : Pro, Ala, Asp, Asn, and Lys) were synthesized using Fmoc‐Rink amide AM SURE resin (0.6 mmol/g, confirmed by Fmoc titration) by solid phase Fmoc chemistry . After building up the final sequence, the samples were Fmoc deprotected and reacted with 5 equivalents of Dabcyl‐OSu, HOBt, and DIPEA at 25 °C for 24 h. Then, each resin was suspended in 3 ml of reagent K, stirred at 25 °C for 1 h and filtered.…”

Section: Methodsmentioning

confidence: 99%

Determination of protease subsite preference on SPOT peptide array by fluorescence quenching‐based assay

Kim

Shin

Lee

2012

Journal of Peptide Science

Self Cite

View full text Add to dashboard Cite

A peptide SPOT array was synthesized on a glass chip and used to determine protease subsite preference. To synthesize a peptide array for positional scanning, the ratio of the isokinetic concentration was determined for every Fmoc-amino acid except Cys. Based on this ratio, a peptide array consisting of Dabcyl-X-X-P(2)-Arg-X-X-X-Lys(FITC) (X: equimolar mixture of 19 amino acids, P(2): one of 19 amino acids) was synthesized on a chitosan-grafted glass chip. Subsequently, the peptide substrates on the array were hydrolyzed by thrombin to screen for subsite specificity using a fluorescence quenching-based assay. The P(2) subsite specificity of thrombin was screened by the fluorescence images obtained after hydrolysis. Pro at the P(2) subsite showed the highest specificity for thrombin based on both the fluorescence quenching-based assay and the solution phase assay. From these results, we confirmed that our mixture-based peptide SPOT array format on the chitosan-grafted glass chips could be used to determine protease subsite preference.

show abstract

Application of AM SURE™ resin to solid-phase peptide synthesis

Cited by 14 publications

References 11 publications

Overview of Solid Phase Synthesis of “Difficult Peptide” Sequences

Overview of Solid Phase Synthesis of “Difficult Peptide” Sequences

Evaluation of COMU as a coupling reagent for in situ neutralization Boc solid phase peptide synthesis

Determination of protease subsite preference on SPOT peptide array by fluorescence quenching‐based assay

Contact Info

Product

Resources

About