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Conformation of an immunoreactive undecapeptide fragment (10–20) of Asp f 1 by NMR and molecular modeling

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Abstract

Allergic bronchopulmonary aspergillosis (ABPA), caused by Aspergillus fumigatus, is a complication of allergic asthma. Asp f 1 secreted by A. fumigatus is reported to be a major allergen/antigen involved in pathogenesis of aspergillosis. A 11-mer immunodominant epitope (Leu-Asn-Pro-Lys-Thr5-Asn-Lys-Trp-Glu-Asp10-Lys) of Asp f 1 has shown immunoreactivity with specific IgG and IgE antibodies in the sera of patients with ABPA in ELISA inhibitionassay. Various studies have suggested that the peptide has a potential use in the development of ELISA based diagnostic kit for early diagnosis of infections caused by A. fumigatus.In view of these interesting properties of the undecapeptide wehave embarked on an investigation of its conformation to understand the relationship between structure and immunoreactivity. NMR and molecular modeling studies of the peptide suggest a structure with a β-turn spanning residuesAsn6 – Glu9 in water at pH 4.0, a β-pleated sheet in DMSO and a α-helix in 40% HFA.

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Authors and Affiliations

  1. Department of Pharmaceutical Chemistry, Bombay College of Pharmacy, Kalina, Mumbai, 400098, India

    P. Desai & E. Coutinho

  2. Tata Institute of Fundamental Research, Homi Bhabha Road, Navy Nagar, Mumbai, 400005, India

    S. Srivastava

  3. Division of Bioploymers, Central Drug Research Institute, Lucknow o[226001, India

    W. Haq & S.B. Katti

Authors
  1. P. Desai
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  2. E. Coutinho
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  3. S. Srivastava
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  4. W. Haq
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  5. S.B. Katti
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Correspondence to E. Coutinho.

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Desai, P., Coutinho, E., Srivastava, S. et al. Conformation of an immunoreactive undecapeptide fragment (10–20) of Asp f 1 by NMR and molecular modeling. Letters in Peptide Science 9, 21–34 (2002). https://doi.org/10.1023/A:1021330515747

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