Adriano Malabarba

Newron Pharmaceuticals (Italy)

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Romeo Ciabatti

Biosearch Technologies (United States)

M Berti

Accademia Italiana Medicina Osteopatica

Pietro Ferrari

Centre International de Recherche sur le Cancer

B. CAVALLERI

Politecnico di Milano

R Pallanza

University of Siena

JÜRGEN KETTENRING

Technion – Israel Institute of Technology

Aldo Trani

Biosearch Technologies (United States)

Paolo Strazzolini

University of Udine

Beth P. Goldstein

Waynesburg University

Jieping Zhu

École Polytechnique Fédérale de Lausanne

Cooperative Institutions

Gruppo CLAS (Italy)

University of Göttingen

Gause Institute of New Antibiotics Russian Academy of Medical Sciences

University of Bologna

Centre National de la Recherche Scientifique

Newron Pharmaceuticals (Italy)

University of Pisa

University of Bari Aldo Moro

Pfizer (United States)

University of Milan

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Section Review Anti-infectives: New approaches to the treatment of vancomycin-resistant bacterial infections

Expert Opinion on Therapeutic Patents (1996)

Adriano Malabarba

AbstractCommercially available glycopeptides Vancomycin (V) and Teicoplanin (T) are drugs of choice for the treatment of methicillin-resistant Staphylococcus aureus (MRSA) and coagulase-negative staphylococci (CNS), which are resistant to beta-lactams and almost all other first-line antibiotics. They are extensively used in the treatment of severe infections caused by multi-resistant Gram-positive pathogens including enterococci. Enterococcal infections have become a dramatic clinical problem since few antibacterial agents are efficacious against these refractory organisms and increasing resistance is rapidly eliminating the current options. The recent emergence and spread of resistance also to glycopeptides in VanA enterococci poses a serious threat for the future. Some strains of methicillin-resistant CNS have reduced susceptibility to T and occasionally to V. Currently, a major concern is the possibility already demonstrated at laboratory level, that high glycopeptide resistance could be transferred from enterococci to staphylococci. It follows that there is an urgent need for new more potent glycopeptides which combine improved activity against methicillin-resistant staphylococci with excellent activity against highly glycopeptide-resistant enterococci (GRE), or alternative drugs effective against these multi-resistant bacteria. This article describes the most recent findings and results achieved in this field with new glycopeptide derivatives and novel approaches based on modifications of the natural glycopeptide-core structure. Other promising investigational drugs potentially useful for overcoming the serious therapeutic problem of glycopeptide-resistant bacterial infections are also reviewed.

Teicoplanin

Glycopeptide antibiotic

10.1517/13543776.6.7.627

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Citations (7)

ChemInform Abstract: Structural Modifications of Glycopeptide Antibiotics

ChemInform (1997)

Adriano Malabarba Thalia I. Nicas R. C. Thompson

Abstract ChemInform is a weekly Abstracting Service, delivering concise information at a glance that was extracted from about 100 leading journals. To access a ChemInform Abstract of an article which was published elsewhere, please select a “Full Text” option. The original article is trackable via the “References” option.

10.1002/chin.199718290

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Teicoplanin, antibiotics from Actinoplanes teichomyceticus nov. sp. VI. Chemical degradation: physico-chemical and biological properties of acid hydrolysis products.

The Journal of Antibiotics (1984)

Adriano Malabarba Paolo Strazzolini A. Depaoli Mauro Landi M Berti

Teicoplanin

Aglycone

Chemical structure

10.7164/antibiotics.37.988

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Citations (86)

Structural Modifications of the Active Site in Teicoplanin and Related Glycopeptides. 1. Reductive Hydrolysis of the 1,2- and 2,3-Peptide Bonds

The Journal of Organic Chemistry (1996)

Adriano Malabarba Romeo Ciabatti JÜRGEN KETTENRING Pietro Ferrari Károly Vékey

Reaction of teicoplanin glycopeptides with sodium borohydride in aqueous ethanol solutions produced open pentapeptide derivatives in which the amide bond between amino acids 2 and 3 was hydrolyzed and the carboxyl group of amino acid 2 was reduced to a primary alcohol. Other glycopeptides of the dalbaheptide family, such as vancomycin, ristocetin, and A-40,926, underwent selective reductive hydrolysis (RH) of the heptapeptide backbone at the same position as in teicoplanins, while antibiotic A-42,867 and vancomycin hexapeptide were resistant. Also, teicoplanin and vancomycin were resistant to RH-treatment when the N-terminus was protected as carbamate. In contrast, open hexapeptides in which the 1,2-peptide bond was hydrolyzed and the carboxyl group of amino acid 1 was reduced to hydroxymethyl were obtained from carbamate derivatives of sugar-free compounds deglucoteicoplanin (TD) and vancomycin−aglycon (VA) under RH-conditions. Limited to BOC or CBZ-TD, the 3,4-amide bond was also affected. A possible RH-mechanism is proposed for natural glycopeptides and their derivatives. Teicoplanin-derived RH penta- and hexapeptides maintained residual antibacterial activity. As other analogous RH-glycopeptides, they are key intermediates for the synthesis of new members of this family of antibiotics. A synthetic approach to ring-closed derivatives of TD hexapeptide alcohol (TDHPA) and their activities are also reported.

Teicoplanin

Peptide bond

Hydroxymethyl

Glycopeptide antibiotic

10.1021/jo941809v

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Citations (24)

Reductive Hydrolysis of the 59,60-Amide Bond of Teicoplanin Antibiotics: A Key Step from Natural to Synthetic Glycopeptides

Journal of Medicinal Chemistry (1994)

Adriano Malabarba Romeo Ciabatti

ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTReductive Hydrolysis of the 59,60-Amide Bond of Teicoplanin Antibiotics: A Key Step from Natural to Synthetic GlycopeptidesAdriano Malabarba and Romeo CiabattiCite this: J. Med. Chem. 1994, 37, 19, 2988–2990Publication Date (Print):September 16, 1994Publication History Published online1 May 2002Published inissue 16 September 1994https://pubs.acs.org/doi/10.1021/jm00045a002https://doi.org/10.1021/jm00045a002research-articleACS PublicationsRequest reuse permissionsArticle Views110Altmetric-Citations16LEARN ABOUT THESE METRICSArticle Views are the COUNTER-compliant sum of full text article downloads since November 2008 (both PDF and HTML) across all institutions and individuals. These metrics are regularly updated to reflect usage leading up to the last few days.Citations are the number of other articles citing this article, calculated by Crossref and updated daily. Find more information about Crossref citation counts.The Altmetric Attention Score is a quantitative measure of the attention that a research article has received online. Clicking on the donut icon will load a page at altmetric.com with additional details about the score and the social media presence for the given article. Find more information on the Altmetric Attention Score and how the score is calculated. Share Add toView InAdd Full Text with ReferenceAdd Description ExportRISCitationCitation and abstractCitation and referencesMore Options Share onFacebookTwitterWechatLinked InRedditEmail Other access optionsGet e-Alertsclose Get e-Alerts

Teicoplanin

Icon

10.1021/jm00045a002

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Citations (19)

[Non-natural aglycones of glycopeptide antibiotics of the vancomycin group. Synthesis and antibacterial activity].

PubMed (1997)

Pavlov AIu Olsuf'eva En Miroshnikova Ov Reznikova Mi Lazhko Ei

A new approach for the modification of the heptapeptide core of glycopeptide antibiotics was proposed based on the replacement of amino acid residues in positions 1 and 3 in teicoplanin aglycone and in position 1 in the eremomycin aglycone. Six novel nonnatural aglycones of the vancomycin type were obtained. Compounds derived from the teicoplanin aglycone exhibited in vitro activity against Gram-positive bacteria, and two of them were also active against the vancomycin-resistant enterococci.

Aglycone

Teicoplanin

Glycopeptide antibiotic

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Citations (2)

BI 397

Drugs of the Future (1999)

Adriano Malabarba Stefano Donadio

10.1358/dof.1999.024.08.545566

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Citations (10)