Snake Venom Peptides and Low Mass Proteins: Molecular Tools and Therapeutic Agents.
Snake venoms are natural sources of biologically active molecules that are able to act selectively and specifically on different cellular targets, modulating physiological functions. Thus, these mixtures, composed mainly of proteins and peptides, provide ample and challenging opportunities and a diversified molecular architecture to design and develop tools and agents of scientific and therapeutic interest. Among these components, peptides and small proteins play diverse roles in numerous physiological processes, exerting a wide range of pharmacological activities, such as antimicrobial, antihypertensive, analgesic, antitumor, analgesic, among others. The pharmaceutical and cosmetic industries have recognized the huge potential of these privileged frameworks and believe them to be a promising alternative to contemporary drugs. A number of natural or synthetic peptides from snake venoms have already found preclinical or clinical applications for the treatment of pain, hypertension, cardiovascular diseases and aging skin. A well-known example is captopril, whose natural peptide precursor was isolated from Bothrops jararaca snake venom, which is a peptide-based drug that inhibits the angiotensin-converting enzyme, producing an anti-hypertensive effect. The present review looks at the main peptides (natriuretic peptides, bradykinin-potentiating peptides and sarafotoxins) and low mass proteins (crotamine, disintegrins and three-Finger toxins) from snake venoms, as well as synthetic peptides inspired by them, describing their biochemical, structural and physiological features, as well as their applications as research tools and therapeutic agents.
Universidad Regional Amazonica Ikiam, Km 7 Via Muyuna, Tena, Napo. Ecuador.
J R
JR
Almeida
Department of Biochemistry and Tissue Biology, Institute of Biology, State University of Campinas (UNICAMP), Campinas, SP. Brazil.
L M
LM
Resende
Universidad Regional Amazonica Ikiam, Km 7 Via Muyuna, Tena, Napo. Ecuador.
R K
RK
Watanabe
Department of Biochemistry and Tissue Biology, Institute of Biology, State University of Campinas (UNICAMP), Campinas, SP. Brazil.
V C
VC
Carregari
Department of Biochemistry and Tissue Biology, Institute of Biology, State University of Campinas (UNICAMP), Campinas, SP. Brazil.
S
S
Huancahuire-Vega
Fiocruz Rondonia, Oswaldo Cruz Foundation (FIOCRUZ), Porto Velho, RO. Brazil.
C A
CA
da S Caldeira
Fiocruz Rondonia, Oswaldo Cruz Foundation (FIOCRUZ), Porto Velho, RO. Brazil.
A
A
Coutinho-Neto
Fiocruz Rondonia, Oswaldo Cruz Foundation (FIOCRUZ), Porto Velho, RO. Brazil.
A M
AM
Soares
UCIBIOREQUIMTE, Department of Chemistry and Biochemistry, Faculty of Sciences, University of Porto. Portugal.
N
N
Vale
UCIBIOREQUIMTE, Department of Chemistry and Biochemistry, Faculty of Sciences, University of Porto. Portugal.
P A
PA
de C Gomes
Department of Biochemistry and Tissue Biology, Institute of Biology, State University of Campinas (UNICAMP), Campinas, SP. Brazil.
S
S
Marangoni
Fiocruz Rondonia, Oswaldo Cruz Foundation (FIOCRUZ), Porto Velho, RO. Brazil.
L
L
de A Calderon
Ikiam - Universidad Regional Amazonica, Km 7, via Muyuna, Tena - Napo. Ecuador.
S L
SL
Da Silva
D000806:Angiotensin-Converting Enzyme Inhibitors / Q000737:chemistry / Q000302:isolation & purification / Q000627:therapeutic use; D000818:Animals; D017837:Bothrops / Q000378:metabolism; D006801:Humans; D006973:Hypertension / Q000188:drug therapy; D010455:Peptides / Q000737:chemistry* / Q000302:isolation & purification / Q000627:therapeutic use; D057786:Peptidomimetics / Q000737:chemistry / Q000627:therapeutic use; D010975:Platelet Aggregation Inhibitors / Q000737:chemistry / Q000302:isolation & purification / Q000627:therapeutic use; D012910:Snake Venoms / Q000737:chemistry*; D013927:Thrombosis / Q000188:drug therapy
D000806:Angiotensin-Converting Enzyme Inhibitors; D010455:Peptides; D057786:Peptidomimetics; D010975:Platelet Aggregation Inhibitors; D012910:Snake Venoms
Crotamine; bradykinin-potentiating peptide; disintegrin; natriuretic peptide; sarafotoxin; three-finger
toxin