Design and synthesis of novel antimicrobial peptides on the basis of α helical domain of Tenecin 1, an insect defensin protein, and structure–activity relationship study

Ahn, Hyun Young; Won-Mi, Cho; Kang, Sunhee; Ko, Sung-Sin; Park, Mi-Sun; Cho, Hyeongjin; Lee, Keun‐Hyeung

doi:10.1016/j.peptides.2005.08.016

Cited by 46 publications

(22 citation statements)

References 35 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Likewise, Ahn et al (2006) developed an AMP based on the 11-residue -helical domain from tenecin 1, an insect defensin isolated from Tenebrio molitor. This -helical domain, named L1, shows no antimicrobial activity.…”

Section: Sequence Template Methods Of Rational Design Of Ampmentioning

confidence: 99%

Prediction and Rational Design of Antimicrobial Peptides

Porto¹,

Franco²

2012

Protein Structure

View full text Add to dashboard Cite

Section: Sequence Template Methods Of Rational Design Of Ampmentioning

confidence: 99%

Prediction and Rational Design of Antimicrobial Peptides

Porto¹,

Franco²

2012

Protein Structure

View full text Add to dashboard Cite

“…Supporting this view is a high overall similarity between the tertiary structures of vertebrate defensins and such toxins as -defensin-like toxins 1 and 2 from platypus venom or the snake (crotalid) myotoxins [9,13,49,217,[234][235][236]. Although there is clear structural similarity observed for vertebrate, insect, and plant defensins, the two latter families are classified within the cysteine-stabilized (CS )-motif [1,10,[237][238][239][240][241][242].…”

Section: Structural Properties Of Human Defensins a Tertiary Stmentioning

confidence: 99%

Human Defensins: Synthesis and Structural Properties

Pazgier

Li²,

Lu³

et al. 2007

CPD

View full text Add to dashboard Cite

Defensins are small, beta-sheet-rich, cationic peptides found in many organisms. All defensins have amphiphilic properties, which are central for antimicrobial activities of the proteins. The human genome encodes many defensin-line molecules, of which 10 have been characterized. Molecules of all known human defensins are stabilized by three intramolecular disulfide bonds arranged in a conserved pattern. To date, studies of human defensins indicate that these proteins are involved in various biological processes associated primarily with defensive and regulatory responses to infections by pathological agents. A comprehensive understanding of the multiple roles played by defensins within the immune system is greatly increased by reviewing the results of detailed structural studies. Emerging structural data, derived by the X-ray crystallography and the NMR spectroscopy in solution combined with functional studies; allow a rational understanding of the different activities of defensins and the mechanisms controlling these activities. Due to their well-established antimicrobial properties, defensins are also being investigated for their potential as therapeutics agents. Recently, increased effort has been focused on studies of the immunoregulatory properties of defensins, associated with their ability to bind and activate the G(i)-protein-coupled seven-transmembrane receptors. Comprehensive studies of defensins require development of simple, efficient, and inexpensive methods to generate these proteins and their derivatives in correctly folded form. This review highlights the current status of the sample generation methods, structural studies, and the structure-function relationships for human defensins.

show abstract

“…solution, without formation of secondary structures such as a helix, which is featured in many other AMPs (Ahn et al, 2006).…”

Section: Treatmentsmentioning

confidence: 99%