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Redalyc.Antimicrobial Peptides: the Role of Hydrophobicity in the Alpha Helical Structure Journal of Pharmacy & Pharmacognosy Research E-ISSN: 0719-4250 [email protected] Asociación de Académicos de Ciencias Farmacéuticas de Antofagasta Chile Perumal, Pandurangan; Pandey, Vijaya P. Antimicrobial peptides: The role of hydrophobicity in the alpha helical structure Journal of Pharmacy & Pharmacognosy Research, vol. 1, núm. 2, noviembre-diciembre, 2013, pp. 39-53 Asociación de Académicos de Ciencias Farmacéuticas de Antofagasta Antofagasta, Chile Available in: http://www.redalyc.org/articulo.oa?id=496050265001 How to cite Complete issue Scientific Information System More information about this article Network of Scientific Journals from Latin America, the Caribbean, Spain and Portugal Journal's homepage in redalyc.org Non-profit academic project, developed under the open access initiative © 2013 Journal of Pharmacy & Pharmacognosy Research, 1 (2), 39-53 ISSN 0719-4250 http://jppres.com/jppres Review | Revisión Antimicrobial peptides: The role of hydrophobicity in the alpha helical structure [Los péptidos antimicrobianos: El papel de la hidrofobicidad en la estructura helicoidal alfa] Pandurangan Perumal*and Vijaya P. Pandey Department of Pharmacy, Annamalai University, Annamalai Nagar, Chidambaram, Tamilnadu, India. * E-mail: [email protected] Abstract Resumen The antimicrobial peptides (AMPs) are a class of molecule obtained Los péptidos antimicrobianos (AMP) son una clase de molécula from plants, insects, animals, and humans. These peptides have been obtenida a partir de plantas, insectos, animales y seres humanos. Estos classified into five categories: 1. Anionic peptide, 2. Linear alpha helical péptidos han sido clasificados en cinco categorías: 1. Péptido aniónico, 2. cationic peptide, 3. Cationic peptide, 4. Anionic and cationic peptides Péptido alfa lineal catiónico helicoidal, 3. Péptido catiónico, 4. Péptidos with disulphide bonds, and 5. Anionic and cationic peptide fragments of aniónicos y catiónicos con enlaces de disulfuro, y 5. Fragmentos de larger proteins. Factors affecting AMPs are sequence, size, charge, péptidos aniónicos y catiónicos de proteínas más grandes. Los factores hydrophobicity, amphipathicity, structure and conformation. Synthesis of que afectan a los AMP son secuencia, tamaño, carga, hidrofobicidad, these peptides is convenient by using solid phase peptide synthesis by anfipaticidad, estructura y conformación. La síntesis de estos péptidos es using FMOC chemistry protocol. The secondary structures of three conveniente mediante el uso de síntesis de péptidos en fase sólida, synthetic peptides were determined by circular dichroism. Also, it was mediante el protocolo de química FMOC. Las estructuras secundarias de compared the stability of the α-helical structure and confirmed the tres péptidos sintéticos se determinaron por dicroísmo circular. También percentage of helix of these peptides by using circular dichroism. Some of ha sido comparada la estabilidad de la estructura α-helicoidal y confir- these AMPs show therapeutic properties like antimicrobial, antiviral, mado el porcentaje de hélice de estos péptidos mediante el uso de contraceptive, and anticancer. The formulations of some peptides have dicroísmo circular. Algunos de estos AMP muestran propiedades terapéu- been entered into the phase I, II, or III of clinical trials. This article to ticas como antibióticas, antivirales, anticonceptivas y anticáncer. Las review briefly the sources, classification, factors affecting AMPs activity, formulaciones de algunos péptidos se encuentran en fases I, II o III de synthesis, characterization, mechanism of action and therapeutic concern ensayos clínicos. Este artículo revisa brevemente las fuentes, clasificación, of AMPs and mainly focussed on percentage of α-helical structure in factores que afectan a la actividad de los AMP, la síntesis, caracterización, various medium. mecanismo de acción y la acción terapéutica de los AMP y se centra principalmente en el porcentaje de la estructura de α-helicoidal en diversos medios. Keywords: Anticancer; antimicrobial peptide; antiviral; circular Palabras Clave: Anticáncer; anticonceptivo; antiviral; dicroismo circular; dichroism; contraceptive. péptido antimicrobiano. List of Abbreviations: AMPs - antimicrobial peptides; BOC - acid labile tertiary butyl oxycarbonyl group; CA-P1,2 or 3 - cecropin-A peptide 1,2 or 3; CD - circular dichroism; DCM – dichloromethane; DIPEA - diiso-propyl ethylamine; DMA - Dimethyl acetamide; DMF - N-N-dimethyl formamide; EL - absorption coefficient of left circularly polarized light; ER - absorption coefficient of right circularly polarized light; FMOC - base labile fluorenyl methyl oxycarbonyl group; HBTU - tetramethyl uranium hexafluorophosphate; HF - hydrogen fluoride; HOBT – Hydroxy benzotriazole; LPPS – Liquid phase peptide synthesis; NPS – 2-nitro phenyl sulfenyl group; PAA – Poly acryl amide; PEG – Poly ethylene glicol; PS – Polystyrene; SDS - sodium dodecylsulphate; SPPS – Solid phase peptide synthesis; TFA - trifluoro acetic acid; TFE – trifluoroethanol; TFMSA - trifluoro methane sulphonic acid. ARTICLE INFO Received | Recibido: November 16, 2013. Received in revised form | Recibido en forma corregida: December 8, 2013. Accepted | Aceptado: December 15, 2013. Available Online | Publicado en Línea: December 31, 2013 Declaration of Interests | Declaración de Intereses: The authors declare that they have no conflict of interests. Funding | Financiación: none stated. _____________________________________ This is an open access article distributed under the terms of a Creative Commons Attribution-Non-Commercial-No Derivative Works 3.0 Unported Licence. (http://creativecommons.org/licenses/by- nc-nd/3.0/ ) which permits to copy, distribute and transmit the work, provided the original work is properly cited. You may not use this work for commercial purposes. You may not alter, transform, or build upon this work. Any of these conditions can be waived if you get permission from the copyright holder. Nothing in this license impairs or restricts the author's moral rights. Este es un artículo de Acceso Libre bajo los términos de una licencia “Creative Commons Atribucion-No Comercial-No trabajos derivados 3.0 Internacional” (http://creativecommons.org/licenses/by-nc-nd/3.0/deed.es) Usted es libre de copiar, distribuir y comunicar públicamente la obra bajo las condiciones siguientes: Reconocimiento. Debe reconocer los créditos de la obra de la manera especificada por el autor o el licenciador (pero no de una manera que sugiera que tiene su apoyo o apoyan el uso que hace de su obra). No comercial. No puede utilizar esta obra para fines comerciales. Sin obras derivadas. No se puede alterar, transformar o generar una obra derivada a partir de esta obra. Al reutilizar o distribuir la obra, tiene que dejar bien claro los términos de la licencia de esta obra. Alguna de estas condiciones puede no aplicarse si se obtiene el permiso del titular de los derechos de autor Nada en esta licencia menoscaba o restringe los derechos morales del autor. Perumal & Pandey Antimicrobial peptides: hydrophobicity and alpha helical structure INTRODUCTION membrane permeabilization to cytoplasm. Riboso- mally-synthesized AMPs, containing only natural Peptides are a class of compounds of low amino acids can be grouped into linear, alpha- molecular weight, which yield amino acids on helical peptides (such as cecropins, magainins, and hydrolysis. The living organisms are constantly mellitin), peptides characterized by enrichment in exposed to the potentially harmful pathogens one or two amino acids (proline arginine-rich through contact, ingestion and inhalation PR39, indolicidin), and peptides containing disulfi- (Hultmark, 2003). While during pathogenic invasion de bonds (e.g., defensins, protegrins). Large num- the first line of defence involves the innate ber of peptides with potent antimicrobial activity immunity followed by acquired immunity (Fearon that were synthesized extra-ribosomally or contain and Locksley, 1996). In contrast of acquired immune substantial post-translational modifications, for mechanism, endogenous peptides (which are in example lipopeptides (polymyxin, dermaseptin) the gastrointestinal, respiratory, and genitourinary and the lantibiotics, which contain non-native tracts), which are induced a fast and effective amino acids or non-peptide backbone structures. defence against pathogens. This group of molecu- In addition, a wide variety of synthetic AMPs have les is termed as ‘antimicrobial peptides’ (AMPs). been developed utilizing either a combinatorial These peptides were found in plants, insects, synthesis approach (Lu et al., 2006; Eckert et al., 2006; animals, and humans (Maróti et al., 2011). The AMPs Gottler and Ramamoorthy, 2009). The aim of this article are short peptides, generally between 12 to 50 to review briefly the sources, classification, factors amino acids present in the sequence of the affecting AMPs activity, synthesis, characteriza- peptides and these peptides are potent, broad tion, mechanism of action and therapeutic spectrum antibiotics, which exhibited potential as concern of AMPs. The second version of the novel therapeutic agents (Zanetti et al., 2002; McPhee antimicrobial peptide database (ADP2) contains and Hancock, 2005; Koczulla and Bals., 2003). These detailed structural information (Wang and Wang, peptides are also called as host defence peptides 2004). (Tossi et al., 2005). Fig. 1 shows the secondary structure of AMPs demonstrated to be effective against antimicrobial peptides such as α-helix
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