Quantitative monitoring of solid-phase peptide synthesis by the ninhydrin reaction

Sarin, Virender K.; Kent, Stephen B. H.; Tam, James P.; Merrifield, R. B.

doi:10.1016/0003-2697(81)90704-1

Cited by 1,056 publications

(648 citation statements)

References 18 publications

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“…The protective group, Dde, of N-Fmoc-Lys (Dde)-OH was removed by incubation with 2% hydrazine monohydrate in dimethylformamide (DMF, 25 ml/g) at room temperature for 3 min. The coupling efficiency (>99%) in every coupling step was determined by measuring residual free amine with the quantitative ninhydrin assay, as previously described (24).…”

Section: Synthesis Of Ligand (S7)mentioning

confidence: 99%

In vitro assessment of the dual-targeting behavior of a peptide-based magnetic resonance imaging contrast agent

Yang

Zhang

et al. 2013

International Journal of Molecular Medicine

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Abstract. In this study, a peptide-based dual-targeting magnetic resonance imaging (MRI) contrast agent (S8) was designed and synthesized. Arg-Gly-Asp (RGD) and Asn-Gly-Arg (NGR) were combined in the targeting vector so as to allow binding, on the surface of tumor cells, to integrin α v β 3 and aminopeptidase N (CD 13 ), respectively. The longitudinal relaxivity (r 1 ) value of S8 was 8.297 mM -1 sec -1 at a magnetic field of 11.7 T, which is approximately double the r 1 value (4.25 mM -1 sec -1 ) of Magnevist, a commercially available contrast agent. MDA-MB-231 human breast cancer cells (which overexpress α v β 3 ) and human prostate cancer cells PC-3 (which overexpress CD 13 ) were used to investigate the tumor-targeting behavior of S8. The results from the present study indicate that the designed contrast agent, S8, targets both MDA-MB-231 and PC-3 cells.

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Section: Synthesis Of Ligand (S7)mentioning

confidence: 99%

In vitro assessment of the dual-targeting behavior of a peptide-based magnetic resonance imaging contrast agent

Yang

Zhang

et al. 2013

International Journal of Molecular Medicine

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“…The Fmoc protecting group was removed using 50% piperidine in dimethylformamide, and dimethylformamide was used as both the coupling solvent and for flow washes throughout the cycle. Where possible, the progress of the assembly was monitored by quantitative ninhydrin monitoring (30). Peptide was deprotected and cleaved from the resin by stirring at room temperature in trifluoroacetic acid:H 2 O:triisopropyl silane: ethanedithiol (90:5:2.5:2.5) for 2-3 h. Cold diethyl ether was then added to the filtered mixture, and the precipitated peptide was collected by centrifugation.…”

mentioning

confidence: 99%

Subtype-selective Noncompetitive or Competitive Inhibition of Human α1-Adrenergic Receptors by ρ-TIA

Chen

Rogge

Hague

et al. 2004

Journal of Biological Chemistry

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The 19-amino acid conopeptide ( -TIA) was shown previously to antagonize noncompetitively ␣ 1B -adrenergic receptors (ARs). Because this is the first peptide ligand for these receptors, we compared its interactions with the three recombinant human ␣ 1 -AR subtypes (␣ 1A , ␣ 1B , and ␣ 1D ). Radioligand binding assays showed that -TIA was 10-fold selective for human ␣ 1B -over ␣ 1A -and ␣ 1D -ARs. As observed with hamster ␣ 1B -ARs, -TIA decreased the number of binding sites (B max ) for human ␣ 1B -ARs without changing affinity (K D ), and this inhibition was unaffected by the length of incubation but was reversed by washing. However, -TIA had opposite effects at human ␣ 1A -ARs and ␣ 1D -ARs, decreasing K D without changing B max , suggesting it acts competitively at these subtypes. -TIA reduced maximal NE-stimulated [ 3 H]inositol phosphate formation in HEK293 cells expressing human ␣ 1B -ARs but competitively inhibited responses in cells expressing ␣ 1A -or ␣ 1D -ARs. Truncation mutants showed that the amino-terminal domains of ␣ 1B -or ␣ 1D -ARs are not involved in interaction with -TIA. Alanine-scanning mutagenesis of -TIA showed F18A had an increased selectivity for ␣ 1B -ARs, and F18N also increased subtype selectivity. I8A had a slightly reduced potency at ␣ 1B -ARs and was found to be a competitive, rather than noncompetitive, inhibitor in both radioligand and functional assays. Thus -TIA noncompetitively inhibits ␣ 1B -ARs but competitively inhibits the other two subtypes, and this selectivity can be increased by mutation. These differential interactions do not involve the receptor amino termini and are not because of the charged nature of the peptide, and isoleucine 8 is critical for its noncompetitive inhibition at ␣ 1B -ARs.

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“…Ninhydrin, Fmoc and trityl tests were carried out by UV spectrophotometry as reported in the literature. 33,37,38 Functionalization of fragmented SU-8: SU-8 (100 mg) was treated with Jeffamine 800 (500 mg, neat) and acetonitrile (500 µl) and heated to 65 o C in an oven overnight. The support was washed with acetonitrile (7 x 800 µl) followed by methanol (7 x 800 µl) and dried under vacuum at room temperature for 4 h to yield 8a and 8b.…”

Section: Su-8 Microfabrication By Photolithographymentioning

confidence: 99%

Multistep Synthesis on SU-8: Combining Microfabrication and Solid-Phase Chemistry on a Single Material

et al. 2007

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SU-8 is an epoxy-novolac resin and a well-established negative photoresist for microfabrication and microengineering. The photopolymerized resist is an extremely highly crosslinked polymer showing outstanding chemical and physical robustness with residual surface epoxy groups amenable for chemical functionalization. In this paper we describe, for the first time, the preparation and surface modification of SU-8 particles shaped as microbars, the attachment of appropriate linkers, and the successful application of these particles to multistep solid-phase synthesis leading to oligonucleotides and peptides attached in an unambiguous manner to the support surface.

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Quantitative monitoring of solid-phase peptide synthesis by the ninhydrin reaction

Cited by 1,056 publications

References 18 publications

In vitro assessment of the dual-targeting behavior of a peptide-based magnetic resonance imaging contrast agent

In vitro assessment of the dual-targeting behavior of a peptide-based magnetic resonance imaging contrast agent

Subtype-selective Noncompetitive or Competitive Inhibition of Human α1-Adrenergic Receptors by ρ-TIA

Multistep Synthesis on SU-8: Combining Microfabrication and Solid-Phase Chemistry on a Single Material

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