Use of Alloc-amino acids in solid-phase peptide synthesis. Tandem deprotection-coupling reactions using neutral conditions

Thieriet, Nathalie; Alsina, Jordi; Giralt, Ernest; Guibé, F.; Alberício, Fernando

doi:10.1016/s0040-4039(97)01690-0

Cited by 156 publications

(145 citation statements)

References 29 publications

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“…The lysine at position 231 was inserted as Lys(alloc), which allowed the selective deprotection of its side chain by Pd catalysis after acetylation of the N-terminal Asp226 (ref. 40). Finally, the Gly-Cys linker was assembled onto the Lys side chain and acetylated to give the full terpyridine-modified peptide attached to the resin.…”

Section: Resultsmentioning

confidence: 99%

Stimuli-responsive selection of target DNA sequences by synthetic bZIP peptides

Mosquera¹,

Jiménez-Balsa²,

Dodero³

et al. 2013

Nat Commun

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One of the strategies used by nature to regulate gene expression relies on the stimulicontrolled combination of DNA-binding proteins. This in turn determines the target-binding site within the genome, and thereby whether a particular gene is activated or repressed. Here we demonstrate how a designed basic region leucine zipper-based peptide can be directed towards two different DNA sequences depending on its dimerization arrangement. While the monomeric peptide is non-functional, a C-terminal metallo-dimer recognizes the natural ATF/CREB-binding site (5 0 -ATGA cg TCAT-3 0 ), and a N-terminal disulphide dimer binds preferentially to the swapped sequence (5 0 -TCAT cg ATGA-3 0 ). As the dimerization mode can be efficiently controlled by appropriate external reagents, it is possible to reversibly drive the peptide to either DNA site in response to such specific inputs. This represents the first example of a designed molecule that can bind to more than one specific DNA sequence depending on changes in its environment.

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Section: Resultsmentioning

confidence: 99%

Stimuli-responsive selection of target DNA sequences by synthetic bZIP peptides

Mosquera¹,

Jiménez-Balsa²,

Dodero³

et al. 2013

Nat Commun

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“…Noteworthy, we used Dglutamic acid derivative 1 as attachment site on the resin to secure the convenient conformation of the template [33]. The removal of Allyl then 9-fluorenylmethoxycarbonyl (Fmoc) protecting group was achieved by typical procedure using respectively PhSiH 3 /Pd(Ph 3 P) 4 [34] and piperidine to afford the linear peptide 3 presenting free N-and C-terminal end.…”

Section: Resultsmentioning

confidence: 99%

A Fully Solid-Phase Synthesis of Biotinylated Glycoclusters

Renaudet¹,

Dumy²

2008

TOGLYJ

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Abstract:The fully solid-phase synthesis of chemically well-defined glycoclusters grafted to a topological cyclodecapeptide template is described. The orthogonally protected peptide backbone was first synthesized and cyclized on solid support using D-glutamic acid as first amino acid linked to the resin. After successive regioselective deprotection steps, biotins were coupled to the lower addressable domains of the scaffold, then carbohydrates-binding ligands were assembled as cluster on the upper domain using a chemoselective oxime-based strategy. This provides multitopic labeled glycopeptides which can be easily immobilized to streptavidin-coated surfaces for studying carbohydrate-protein interactions in glycomic researches.

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“…One amino group would be protected by the standard Fmoc ( ¼ 9-fluorenylmethoxycarbonyl) protecting group for immediate functionalization, while the second would be blocked by the Alloc ( ¼ allyloxycarbonyl) protecting group, which is resistant to piperidine and can be removed selectively under neutral conditions with Pd(PPh 3 ) 4 and phenyltrihydrosilane (PhSiH 3 ). [13] The chiral branching diamino acid 1 was prepared in eight steps from commercially available (R)-N-tert-butyloxycarbonyl-3-aminopropane-1,2-diol 3, in an overall yield of 23% (Scheme 2). Thus, protection of the amino group in 3 with Boc 2 O gave 4.…”

Section: Synthesismentioning

confidence: 99%

“…The Alloc protecting group at the level of the first branching unit was removed by treatment with tetrakis(triphenylphosphine)palladium(0) and phenylsilane. [13] The fourth amino acid A 4 was introduced, followed again by the asymmetric branching unit 1. Fmoc deprotection then allowed us to couple a single copy of an amino acid at position A 5 , which was acetylated.…”

Section: Synthesismentioning

confidence: 99%

Esterolytic Peptide Dendrimers with a Hydrophobic Core and Catalytic Residues at the Surface

2004

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(3S)-4-(9-Fluorenylmethoxycarbonylamino)-3-methyl(allyloxycarbonyl)aminoethyloxyacetic acid (1) was prepared from (R)-3-aminopropane-1,2-diol and used as branching unit for the synthesis of second generation peptide dendrimers with six individually addressable variable amino acid positions. Three pairs of diastereomeric dendrimers were prepared bearing a common hydrophobic core and permutations of the catalytic triad amino acids aspartate, histidine and serine at the surface. Dendrimers with two surface histidine residues catalyzed the hydrolysis of fluorogenic 8-acyloxypyrene-1,3,6-trisulfonates in aqueous buffer pH 6.0 with rate enhancement k cat /k uncat in the 10 3 range and Michaelis-Menten constants K M in the 10 À 4 M range. Substrate recognition involves electrostatic interactions, as shown by competitive inhibition of catalysis observed with pyrene-1,3,6,8-tetrasulfonate. The 4-fold to 7-fold lowering in K M between the butyryl and nonanoyl esters in the most active dendrimers provides evidence for a hydrophobic component in substrate binding, which is absent in a closely related, less active diastereomeric peptide dendrimer.

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Use of Alloc-amino acids in solid-phase peptide synthesis. Tandem deprotection-coupling reactions using neutral conditions

Cited by 156 publications

References 29 publications

Stimuli-responsive selection of target DNA sequences by synthetic bZIP peptides

Stimuli-responsive selection of target DNA sequences by synthetic bZIP peptides

A Fully Solid-Phase Synthesis of Biotinylated Glycoclusters

Esterolytic Peptide Dendrimers with a Hydrophobic Core and Catalytic Residues at the Surface

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