The 2,2,4,6,7-pentamethyldihydrobenzofuran-5-sulfonyl group (Pbf) as arginine side chain protectant

Carpino, Louis A.; Shroff, Hitesh N.; Triolo, Salvatore A.; Mansour, E. M. E.; Wenschuh, Holger; Alberício, Fernando

doi:10.1016/s0040-4039(00)61487-9

Cited by 121 publications

(83 citation statements)

References 16 publications

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“…[15,16] Many different protecting groups based on nitro, urethane, arylsulphonyl or aryl derivatives have been proposed, but so far none of them satisfies the basic requirements for an ideal protecting group, that is, robust protection to prevent undesired side reactions, and clean and smooth removal under mild conditions. [16] Nevertheless, acid-labile protections, such as N -bis(Boc), N w -Pmc [17] or N w -Pbf [18] are reported to be amenable to solidphase peptide synthesis using the Fmoc strategy.…”

Section: Resultsmentioning

confidence: 99%

Design, Synthesis and Structural Investigations of a β‐Peptide Forming a 3₁₄‐Helix Stabilized by Electrostatic Interactions

Rueping

Mahajan

Jaun

et al. 2004

Chemistry A European J

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Two different strategies have been employed for the synthesis of Fmoc-protected beta(3)-homoarginine; the Arndt-Eistert homologation of alpha-arginine and the guanidinylation of beta(3)-homoornithine. Solid-phase beta-peptide synthesis was used for the preparation of beta-heptapeptide 1, which was designed to form a helix stabilized by electrostatic interactions through positively (beta(3)hArg) and negatively charged (beta(3)hGlu) amino acid residues. CD measurements and corresponding NMR investigations in MeOH and aqueous solutions do indeed show that the beta-peptidic 3(14)-helix can be stabilized by salt-bridge formation.

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Section: Resultsmentioning

confidence: 99%

Design, Synthesis and Structural Investigations of a β‐Peptide Forming a 3₁₄‐Helix Stabilized by Electrostatic Interactions

Rueping

Mahajan

Jaun

et al. 2004

Chemistry A European J

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“…38 for example) using Fmoc for ␣-protection (39), tert-butyl type groups for side chain protection, and trityl for cysteine. Arginine was used under its protected form, 2,2,4,6,7-pentamethyldihydrobenzofuran-5-sulfonyl arginine (40). Final deprotection and cleavage from the resin was achieved by treatment with 90% trifluoroacetic acid in the presence of thiol scavengers.…”

Section: Methodsmentioning

confidence: 99%

Structure-Activity Relationship Studies of Melanin-concentrating Hormone (MCH)-related Peptide Ligands at SLC-1, the Human MCH Receptor

Audinot

Beauverger

Lahaye

et al. 2001

Journal of Biological Chemistry

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Melanin-concentrating hormone (MCH) is a cyclic nona- Melanin-concentrating hormone (MCH)1 has been initially described in fish as a heptadecapeptide (Asp-Thr-Met-Arg-CysMet-Val-Gly-Arg-Val-Tyr-Arg-Pro-Cys-Trp-Glu-Val (1)). Its structure was relatively conserved throughout evolution, although in mammals the sequence of MCH is a nonadecapeptide with differences mainly in the N terminus (Asp-Phe-Asp-MetLeu-Arg-Cys-Met-Leu-Gly-Arg-Val-Tyr-Arg-Pro-Cys-Trp-GlnVal (2)). In rodents, there are now several lines of evidence for the involvement of MCH in the central regulation of feeding behavior as reviewed by Tritos and Maratos-Flier (3). The MCH peptide and its receptor are expressed in the hypothalamus, a region involved in energy balance and food intake (4 -7). In this particular brain area, MCH mRNA is overexpressed and up-regulated during fasting in ob/ob mice as well as in rats (8, 9). Intra-cerebroventricular injections of MCH promote feeding in mice and rats (9 -12). Finally, transgenic mice lacking the MCH gene are lean and hypophagic (13). Interestingly, in peripheral tissues, MCH also stimulates the release of leptin from isolated rat adipocytes (14). The lack of suitable binding conditions, mainly due to the hydrophobic and sticky nature of MCH itself or derivatives (15, 16), was probably a limitation for expression cloning of the receptor. The MCH receptor was nevertheless recently identified by several groups using reverse pharmacology (17-21). The MCH function was assigned to the previously described orphan receptor SLC-1 (22, 23), using inhibition of forskolin-stimulated cAMP production and induction of calcium rise.Receptor cloning and association of functional tests open the way to the search for pharmacological tools, especially receptor antagonists that are needed to study receptor functions. One of the possible strategies to this goal is the chemical modification of the natural peptide including peptide shortening, amino acid substitution, and conformation restriction with the help of structure-activity relationships and modeling studies toward optimized nonpeptide ligands. Such a strategy has been successful for the design of subtype-specific antagonists of neuropeptide Y receptors (24 -27).In the case of MCH, only two sets of data have been published on the pharmacological action and binding affinity of MCH analogues in vitro. A first series of experiments with fish MCH on fish, frog, or other batrachian skin assays were reported (28 -32), showing that fish MCH could be shortened at * This work was supported by a a Convention CIFRE between the Association Nationale de la Recherche Technique, the Institut de Recherches SERVIER and the Centre National de la Recherche Scientifique (to T. S.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.*

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“…Then, the resulting white precipitate was collected through filtration and washed three times with water; 2) Gua-SS-PAAs-Pbf-Cl was synthesized by Michael addition between CBA and CAR/CHL-Pbf-Cl according to a previous report. 24 After oven-drying overnight, the white precipitate (CAR-Pbf-Cl/CHL-Pbf-Cl, 0.76 mmol, and 0.24/0.60 g) and CBA (0.38 mmol, 0.1 g) were added to a brown flask and dissolved with N,N-dimethylformamide (5 mL). The reaction solution was then placed in a temperature-controlled water bath at 60°C under nitrogen atmosphere and was stirred continuously in the dark for at least 6 days.…”

Section: Synthesis Of Gua-ss-paasmentioning

confidence: 99%

Guanidinylated bioresponsive poly(amido amine)s designed for intranuclear gene delivery

Zhang

Xing

et al. 2016

IJN

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Guanidinylated poly(amido amine)s with multiple disulfide linkages (Gua-SS-PAAs) were designed and constructed as nonviral gene carriers. The main chains of these novel carriers were synthesized based on monomers containing guanidino groups (guanidine hydrochloride and chlorhexidine), which could avoid complicated side-chain-modification reactions while introducing the guanidino groups. The synthesized Gua-SS-PAAs polymers were characterized by 1 H nuclear magnetic resonance, molecular weight, and polydispersity. Furthermore, Gua-SS-PAAs polymers were complexed with p DNA, and the properties of the complexes were determined, including entrapment efficiency, particle size, ζ -potential, atomic force microscopy images, stability, DNA complexation ability, reduction sensitivity, cytotoxicity, and transfection efficiency. The new Gua-SS-PAAs carriers exhibited higher transfection efficiency and lower cytotoxicity compared with two widely used gene delivery carriers, polyethylenimine and lipofectamine 2000. Furthermore, the relationship between the side-chain structure and morphological/biological properties was extrapolated, and the results showed that guanidine in the side chain aids in the improvement of transfection efficiency. In addition, the introduction of guanidino group might confer the new carriers with nuclear localization function compared to carriers without it.

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The 2,2,4,6,7-pentamethyldihydrobenzofuran-5-sulfonyl group (Pbf) as arginine side chain protectant

Cited by 121 publications

References 16 publications

Design, Synthesis and Structural Investigations of a β‐Peptide Forming a 3₁₄‐Helix Stabilized by Electrostatic Interactions

Design, Synthesis and Structural Investigations of a β‐Peptide Forming a 3₁₄‐Helix Stabilized by Electrostatic Interactions

Structure-Activity Relationship Studies of Melanin-concentrating Hormone (MCH)-related Peptide Ligands at SLC-1, the Human MCH Receptor

Guanidinylated bioresponsive poly(amido amine)s designed for intranuclear gene delivery

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The 2,2,4,6,7-pentamethyldihydrobenzofuran-5-sulfonyl group (Pbf) as arginine side chain protectant

Cited by 121 publications

References 16 publications

Design, Synthesis and Structural Investigations of a β‐Peptide Forming a 314‐Helix Stabilized by Electrostatic Interactions

Design, Synthesis and Structural Investigations of a β‐Peptide Forming a 314‐Helix Stabilized by Electrostatic Interactions

Structure-Activity Relationship Studies of Melanin-concentrating Hormone (MCH)-related Peptide Ligands at SLC-1, the Human MCH Receptor

Guanidinylated bioresponsive poly(amido amine)s designed for intranuclear gene delivery

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Product

Resources

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Design, Synthesis and Structural Investigations of a β‐Peptide Forming a 3₁₄‐Helix Stabilized by Electrostatic Interactions

Design, Synthesis and Structural Investigations of a β‐Peptide Forming a 3₁₄‐Helix Stabilized by Electrostatic Interactions