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008			141021s2015 xxu| s |||| 0|eng d
020			_a9781493910106
024	7		_a10.1007/978-1-4939-1010-6 _2doi
040			_dES-MaUEC
050		4	_aQP552.P4 _bL593 2015
100	1		_aLi, Yanyan _0Local _993432
245	1	0	_aLasso Peptides : _bBacterial Strategies to Make and Maintain Bioactive Entangled Scaffolds _cby Yanyan Li, Séverine Zirah, Sylvie Rebuffat
260			_aNew York _bSpringer International Publishing _c2015
300			_a1 recurso en línea (XIII, 103 p.) _b22 ilustraciones, 9 ilustraciones en color
336			_aTexto (visual) _btxt _2rdacontent
337			_aelectrónico _bc _2rdamedia
338			_arecurso electrónico _bcr _2rdacarrier
490	0		_aSpringerBriefs in Microbiology _x2191-5385
505	0		_aOverview on Lasso Peptide Research -- From the Producer Microorganisms to the Lasso Scaffold -- Biological Activities of Lasso Peptides and Structure-Activity Relationships -- Biosynthesis, Regulation and Export of Lasso Peptides -- Lasso Peptide Bioengineering and Bioprospecting.
520			_aLasso peptides form a growing family of fascinating ribosomally-synthesized and post-translationally modified peptides produced by bacteria. They contain 15 to 24 residues and share a unique interlocked topology that involves an N-terminal 7 to 9-residue macrolactam ring where the C-terminal tail is threaded and irreversibly trapped. The ring results from the condensation of the N-terminal amino group with a side-chain carboxylate of a glutamate at position 8 or 9, or an aspartate at position 7, 8 or 9. The trapping of the tail involves bulky amino acids located in the tail below and above the ring and/or disulfide bridges connecting the ring and the tail. Lasso peptides are subdivided into three subtypes depending on the absence (class II) or presence of one (class III) or two (class I) disulfide bridges. The lasso topology results in highly compact structures that give to lasso peptides an extraordinary stability towards both protease degradation and denaturing conditions. Lasso peptides are generally receptor antagonists, enzyme inhibitors and/or antibacterial or antiviral (anti-HIV) agents. The lasso scaffold and the associated biological activities shown by lasso peptides on different key targets make them promising molecules with high therapeutic potential. Their application in drug design has been exemplified by the development of an integrin antagonist based on a lasso peptide scaffold. The biosynthesis machinery of lasso peptides is therefore of high biotechnological interest, especially since such highly compact and stable structures have to date revealed inaccessible by peptide synthesis. Lasso peptides are produced from a linear precursor LasA, which undergoes a maturation process involving several steps, in particular cleavage of the leader peptide and cyclization. The post-translational modifications are ensured by a dedicated enzymatic machinery, which is composed of an ATP-dependent cysteine protease (LasB) and a lactam synthetase (LasC) that form an enzymatic complex called lasso synthetase. Microcin J25, produced by Escherichia coli AY25, is the archetype of lasso peptides and the most extensively studied. To date only around forty lasso peptides have been isolated, but genome mining approaches have revealed that they are widely distributed among Proteobacteria and Actinobacteria, particularly in Streptomyces, making available a rich resource of novel lasso peptides and enzyme machineries towards lasso topologies.
650		7	_2embne _9146243 _aPéptidos
700	1		_aZirah, Séverine _993433 _0Local
700	1		_aRebuffat, Sylvie _993434 _0Local
856	4	0	_uhttps://go.openathens.net/redirector/universidadeuropea.es?url=https://link.springer.com/book/10.1007/978-1-4939-1010-6 _zAcceso a este recurso digital (usuarios Universidad Europea de Madrid)
907			_a.b12897553 _b10-10-17 _c18-01-16
942			_2lcc _cLE
945			_aQP552.P4 L593 2015 EB _g1 _ieBOOK _j0 _lmae _o- _pEUR0.00 _q- _r- _sb _t15 _u0 _v0 _w0 _x0 _y.i1156717x _z06-04-17
988			_aEBSPRINGER
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