<i>S</i>‐ and <i>C</i>‐glycopeptide derivatives of an LH‐RH agonist

Michael, Katja; Wittmann, Valentin; König, Wolfgang; Sandow, J.; Kessler, Horst

doi:10.1111/j.1399-3011.1996.tb01107.x

Cited by 28 publications

(3 citation statements)

References 73 publications

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“…An S-glycosylated amino acid derivative has been synthesized by glycosylation of a D-cysteine derivative with the L-rhamnosyl trichloroacetimidate [209]. The Sglycosyl amino acid was used for the synthesis of an 5'-glycopeptide derivative of a luteinizing hormone-releasing hormone (LH-RH) antagonist.…”

Section: S-glycosidesmentioning

confidence: 99%

Trichloroacetimidates

Schmidt¹,

Jung²

2000

Carbohydrates in Chemistry and Biology

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Section: S-glycosidesmentioning

confidence: 99%

Trichloroacetimidates

Schmidt¹,

Jung²

2000

Carbohydrates in Chemistry and Biology

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“…This work has now led us to explore the influence of glycosylation on the cellular uptake, taking as a starting point our lead (R6/W3) CPP sequence [19][20][21]. Glycosylation of bioactive compounds has been used mainly for increasing either the hydrophilicity, the enzymatic stability of the compound, and/or its delivery into the brain [22][23][24][25]. In the context of CPPs, we have hypothesized that glycosylation may regulate and or affect the internalization of the corresponding glycosylated analogs of (R6/W3) [26][27][28][29][30].…”

Section: Introductionmentioning

confidence: 99%

Glycosylated cell-penetrating peptides and their conjugates to a proapoptotic peptide: preparation by click chemistry and cell viability studies

et al. 2009

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Cell-penetrating peptides (CPPs), which are usually short basic peptides, are able to cross cell membranes and convey bioactive cargoes inside cells. CPPs have been widely used to deliver inside cells peptides, proteins, and oligonucleotides; however, their entry mechanisms still remain controversial. A major problem concerning CPPs remains their lack of selectivity to target a specific type of cell and/or an intracellular component. We have previously shown that myristoylation of one of these CPPs affected the intracellular distribution of the cargo. We report here on the synthesis of glycosylated analogs of the cell-penetrating peptide (R6/W3): Ac-RRWWRRWRR-NH 2 . One, two, or three galactose(s), with or without a spacer, were introduced into the sequence of this nonapeptide via a triazole link, the Huisgen reaction being achieved on a solid support. Four of these glycosylated CPPs were coupled via a disulfide bridge to the proapoptotic KLAK peptide, (KLAKLAKKLAKLAK), which alone does not enter into cells. The effect on cell viability and the uptake efficiency of different glycosylated conjugates were studied on CHO cells and were compared to those of the nonglycosylated conjugates: (R6/W3)S-S-KLAK and penetratinS-S-KLAK. We show that glycosylation significantly increases the cell viability of CHO cells compared to the nonglycosylated conjugates and concomitantly decreases the internalization of the KLAK cargo. These results suggest that glycosylation of CPP may be a key point in targeting specific cells.

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“…Despite early reports on the use of free radical reactions for the synthesis of C-glycosyl amino acids and peptides [86,105], this approach is still rarely used in comparison to the above-mentioned nucleophilic approaches. Linker et al reported a short three-step synthesis of 2-C-branched glyco-amino acids by addition of nitroacetate to various glycals in the presence of ceric(IV) ammonium nitrate and subsequent reduction of the obtained bicyclic isoxazoline N-oxides [106].…”

Section: Scheme 13 Synthetic Route To C-mannopyranosyl Phenylalanine 68mentioning

confidence: 99%