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Spider venoms: a rich source of acylpolyamines and peptides as new leads for CNS drugs.
Nat Prod Rep. 2007 Feb; 24(1):145-61.NP

Abstract

Advances in NMR and mass spectrometry as well as in peptide biochemistry coupled to modern methods in electrophysiology have permitted the isolation and identification of numerous products from spider venoms, previously explored due to technical limitations. The chemical composition of spider venoms is diverse, ranging from low molecular weight organic compounds such as acylpolyamines to complex peptides. First, acylpolyamines (< 1000 Da) have an aromatic moiety linked to a hydrophilic lateral chain. They were characterized for the first time in spider venoms and are ligand-gated ion channel antagonists, which block mainly postsynaptic glutamate receptors in invertebrate and vertebrate nervous systems. Acylpolyamines represent the vast majority of organic components from the spider venom. Acylpolyamine analogues have proven to suppress hippocampal epileptic discharges. Moreover, acylpolyamines could suppress excitatory postsynaptic currents inducing Ca+ accumulation in neurons leading to protection against a brain ischemic insult. Second, short spider peptides (< 6000 Da) modulate ionic currents in Ca2+, Na+, or K+ voltage-gated ion channels. Such peptides may contain from three to four disulfide bridges. Some spider peptides act specifically to discriminate among Ca2+, Na+, or K+ ion channel subtypes. Their selective affinities for ion channel subfamilies are functional for mapping excitable cells. Furthermore, several of these peptides have proven to hyperpolarize peripheral neurons, which are associated with supplying sensation to the skin and skeletal muscles. Some spider N-type calcium ion channel blockers may be important for the treatment of chronic pain. A special group of spider peptides are the amphipathic and positively charged peptides. Their secondary structure is alpha-helical and they insert into the lipid cell membrane of eukaryotic or prokaryotic cells leading to the formation of pores and subsequently depolarizing the cell membrane. Acylpolyamines and peptides from spider venoms represent an interesting source of molecules for the design of novel pharmaceutical drugs.

Authors+Show Affiliations

Instituto de Biotecnología, UNAM, Avenida Universidad 2001, Cuernavaca, Morelos 62210, México.No affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't
Review

Language

eng

PubMed ID

17268611

Citation

Estrada, Georgina, et al. "Spider Venoms: a Rich Source of Acylpolyamines and Peptides as New Leads for CNS Drugs." Natural Product Reports, vol. 24, no. 1, 2007, pp. 145-61.
Estrada G, Villegas E, Corzo G. Spider venoms: a rich source of acylpolyamines and peptides as new leads for CNS drugs. Nat Prod Rep. 2007;24(1):145-61.
Estrada, G., Villegas, E., & Corzo, G. (2007). Spider venoms: a rich source of acylpolyamines and peptides as new leads for CNS drugs. Natural Product Reports, 24(1), 145-61.
Estrada G, Villegas E, Corzo G. Spider Venoms: a Rich Source of Acylpolyamines and Peptides as New Leads for CNS Drugs. Nat Prod Rep. 2007;24(1):145-61. PubMed PMID: 17268611.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Spider venoms: a rich source of acylpolyamines and peptides as new leads for CNS drugs. AU - Estrada,Georgina, AU - Villegas,Elba, AU - Corzo,Gerardo, Y1 - 2006/12/06/ PY - 2007/2/3/pubmed PY - 2007/3/14/medline PY - 2007/2/3/entrez SP - 145 EP - 61 JF - Natural product reports JO - Nat Prod Rep VL - 24 IS - 1 N2 - Advances in NMR and mass spectrometry as well as in peptide biochemistry coupled to modern methods in electrophysiology have permitted the isolation and identification of numerous products from spider venoms, previously explored due to technical limitations. The chemical composition of spider venoms is diverse, ranging from low molecular weight organic compounds such as acylpolyamines to complex peptides. First, acylpolyamines (< 1000 Da) have an aromatic moiety linked to a hydrophilic lateral chain. They were characterized for the first time in spider venoms and are ligand-gated ion channel antagonists, which block mainly postsynaptic glutamate receptors in invertebrate and vertebrate nervous systems. Acylpolyamines represent the vast majority of organic components from the spider venom. Acylpolyamine analogues have proven to suppress hippocampal epileptic discharges. Moreover, acylpolyamines could suppress excitatory postsynaptic currents inducing Ca+ accumulation in neurons leading to protection against a brain ischemic insult. Second, short spider peptides (< 6000 Da) modulate ionic currents in Ca2+, Na+, or K+ voltage-gated ion channels. Such peptides may contain from three to four disulfide bridges. Some spider peptides act specifically to discriminate among Ca2+, Na+, or K+ ion channel subtypes. Their selective affinities for ion channel subfamilies are functional for mapping excitable cells. Furthermore, several of these peptides have proven to hyperpolarize peripheral neurons, which are associated with supplying sensation to the skin and skeletal muscles. Some spider N-type calcium ion channel blockers may be important for the treatment of chronic pain. A special group of spider peptides are the amphipathic and positively charged peptides. Their secondary structure is alpha-helical and they insert into the lipid cell membrane of eukaryotic or prokaryotic cells leading to the formation of pores and subsequently depolarizing the cell membrane. Acylpolyamines and peptides from spider venoms represent an interesting source of molecules for the design of novel pharmaceutical drugs. SN - 0265-0568 UR - https://www.unboundmedicine.com/medline/citation/17268611/Spider_venoms:_a_rich_source_of_acylpolyamines_and_peptides_as_new_leads_for_CNS_drugs_ L2 - https://doi.org/10.1039/b603083c DB - PRIME DP - Unbound Medicine ER -