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119. Ladbury JE (2010) Calorimetry as a tool for understanding biomolecular interactions and an aid to drug design. Biochem Soc Trans 38: 888-893. 120. Shrivastava T, Dey A, Ramachandran R (2009) Ligand-induced structural transitions, mutational analysis, and ‘open’ quaternary structure of M. tuberculosis feast/famine regulatory protein (Rv3291c). JMB 392: 1007-1019. 121. Falconer RJ, Penkova A, Jelesarov I, Collins BM (2010) Survey of the year 2008: applications of isothermal titration calorimetry. J Mol Recognit 23: 395-413. 122. BjeliÄ‡ S, Jelesarov I (2008) A survey of the year 2007 literature on applications of isothermal titration calorimetry. J Mol Recognit 21: 289-312. 123. Johnson CM (2013) Differential scanning calorimetry as a tool for protein folding and stability. Arch Biochem Biophys 531: 100-109. 124. Jelesarov I, Bosshard HR (1999) Isothermal titration calorimetry and differential scanning calorimetry as complementary tools to investigate the energetics of biomolecular recognition. J Mol Recognit 12: 3-18. 125. Chiu MH, Prenner EJ (2011) Differential scanning calorimetry: An invaluable tool for a detailed thermodynamic characterization of macromolecules and their interactions. J Pharm Bioallied Sci 3: 39-59. 126. Celej MS, Montich GG, Fidelio GD (2003) Protein stability induced by ligand binding correlates with changes in protein flexibility. Protein Sci 12: 1496-1506. 127. Celej MS, Dassie SA, González M, Bianconi ML, Fidelio GD (2006) Differential scanning calorimetry as a tool to estimate binding parameters in multiligand binding proteins. Anal Biochem 350: 277-284. 128. Bruylants G, Wouters J, Michaux C (2005) Differential scanning calorimetry in life science: thermodynamics, stability, molecular recognition and application in drug design. Curr Med Chem 12: 2011-2020. 129. Cañadas O, Casals C (2013) Differential scanning calorimetry of protein-lipid interactions. Methods Mol Biol 974: 55-71. 130. Dragan AI, Klass J, Read C, Churchill ME, Crane-Robinson C, et al. (2003) DNA binding of a non-sequence-specific HMG-D protein is entropy driven with a substantial non-electrostatic contribution. J Mol Biol 331: 795-813. 131. Dragan AI, Read CM, Makeyeva EN, Milgotina EI, Churchill ME, et al. (2004) DNA binding and bending by HMG boxes: energetic determinants of specificity. J Mol Biol 343: 371-393. OMICS Group eBooks 018
New Peptide Based Therapeutic Approaches Riyasat Ali 1 *, Richa Rani 2 and Sudhir Kumar 3 1 Department of Biochemistry, All India Institute of Medical Sciences, New Delhi 110029, India 2Department of Biotechnology, Indian Institute of Technology, Roorkee 247667, Uttarakhand, India 3 Department of Environmental Health, College of Medicine, University of Cincinnati, Cincinnati, OH 45267-0056, USA *Corresponding author: Riyasat Ali, Department of Biochemistry, All India Institute of Medical Sciences, New Delhi 110029, India, E-mail: riyasataiims@gmail.com Abstract A large number of chemically well defined and synthetic linear as well as branched therapeutics peptides have been developed and used for a large number of therapeutic applications. Peptides and peptide analogues have been developed to mimic naturally occurring molecules like hormones; growth factors etc. along with recently developed several peptide inhibitors. Moreover, large numbers of studies have been performed to establish peptides as an immune prophylactic and immune diagnostic for several infectious diseases like malaria, HIV and plague etc. Synthetic peptide approach have been popularised due to its ease of synthesising large amount of peptides and liberty to modify peptides in order to make them more effective. In the last couple of decades, with the advancement of technology, it has become easy to synthesise longer peptides using peptide conjugation and modification strategies. Moreover, wide range of targeted delivery vehicles of peptides using several bio-compatible polymers have been developed which made peptide drug approach more popular for therapeutic purposes. Targeted and drug release kinetics for optimum drug dispensing have been greatly advanced which increases bio-availability and stability of peptides in the system for longer therapeutic effects. Introduction The enormous increase in the cost and time span to develop a conventional drugs led researchers and pharmaceutical companies to develop new cost-effective products based of synthetic peptide strategy, which led us to develop large number of peptides of medical importance. Although, peptides are generally considered to be poor drug candidates because of their low oral bioavailability and propensity to be rapidly metabolized, yet development of synthetic single and/or linear peptides was found to be a remarkable advancement for drug discovery and therapeutics. In the past, a large number of potent peptide drugs have been developed as chemically defined or recombinant peptides. Although peptides have several advantages over small molecules and antibodies, there are some limitations associated with peptides which limit their use as a mainstream drug source. Firstly, they exhibit low potency and short half life, owing to rapid renal clearance, and lack in vivo stability due to protease degradation. Secondly, peptides also exhibit limited access to the intracellular space and can contain potential immunogenic sequences (random peptides) in general. Therapeutic peptides traditionally have been derived from three sources: (i) natural or bioactive peptides produced by plants, animal or human (derived from naturally occurring peptide hormones or from fragments of larger proteins); (ii) peptides isolated from genetic or recombinant libraries and (iii) peptides discovered from chemical libraries. With the advancement of peptide synthesis technologies, improved productivity and reduced metabolism of peptides, along with alternative routes of administration, several bioactive peptides have been developed which are found to be highly functional with many serving as potent agonists and antagonists against several receptors involved in disease progression. Therapeutic peptides contribute significantly to the treatment of diabetic, osteoporotic, oncologic, gastroenterologic, cardiovascular, immunosuppression, acromegaly, enuresis, antiviral, obesity, antibacterial and antifungal indications (Table 1). On the other hand, a large number of immuno-prophylactic and immuno-diagnostic peptides have also been developed for several infectious diseases like HIV, Malaria, plague, influenza, anthrax and autoimmune diseases like Type 1 Diabetes etc. Although, there is an immense development in the field of peptide chemistry yet it has been associated with many difficulties which are related to the stability of peptides in the system, structure and sometimes immunogenicity of long peptides, that we are not interested. To use peptide as a therapeutic peptide, its biological activity, pharmacokinetic profile and low immunogenicity are crucial parameters. Various chemical modifications have been employed to overcome these limitations of peptides. Many cyclic peptides, pseudo-peptides (modification of the peptide bond) and peptidomimetics (non-peptide molecules) preserving the biological properties of peptides have been developed to increase their stability and bioavailability. However, targeted delivery of therapeutic peptides is still a challenging task. Many therapeutic peptides and peptide analogues do not have ideal delivery and release kinetics and hence new delivery system need to be developed which can ideally suited pharmacokinetics, bioavailability and toxicity profiles as well. In addition, peptide delivery profile/efficacy has been developed taking various pharmacokinetic parameters like extended release, pulsatile delivery, increased bioavailability and renal clearance. Furthermore, various routes of delivery (transdermal, pulmonary, nasal and oral) of peptide have been developed recently. OMICS Group eBooks 003
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Tyrosine Nitrated Proteins: Biochem
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[58-61]. Protein sulfhydryls [62] a
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Oligoclonality of the antibody resp
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The Recent Methodologies of Protein
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are due to altering protein activit
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Figure 6: At Domain Level, Protein
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Brownian Dynamics (BD) method Prote
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protein demonstrate the lowest ener
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Figure 12: Steps in Protein Prepara
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FlexServ The flexibility of protein
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Advances in Protein Thermodynamics
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Figure 12: Residue Clusters with Mu
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Figure 16: Various Features at the
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Advances in Protein Chemistry Chapt
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MMPs are believed to remodel the EC
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MMPs7 (Matrilysin, PUMP 1) A big ro
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Proteins and Peptides- Reemergence
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