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AHTPDB: a comprehensive platform for analysis and presentation of antihypertensive peptides.

Kumar R, Chaudhary K, Sharma M, Nagpal G, Chauhan JS, Singh S, Gautam A, Raghava GP - Nucleic Acids Res. (2014)

Bottom Line: In addition, the database provides structural information of these peptides that includes predicted tertiary and secondary structures.A user-friendly web interface with various tools has been developed to retrieve and analyse the data.It is anticipated that AHTPDB will be a useful and unique resource for the researchers working in the field of antihypertensive peptides.

View Article: PubMed Central - PubMed

Affiliation: Bioinformatics Centre, CSIR-Institute of Microbial Technology, Chandigarh 160036, India.

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Distribution of antihypertensive peptides in AHTPDB database based on various sources.
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Figure 2: Distribution of antihypertensive peptides in AHTPDB database based on various sources.

Mentions: AHTPs have been isolated from various sources, including natural food, fungi, algae, microorganism, insects or snake venom. Among natural food sources, milk is the most explored source for identification of AHTPs with 834 entries (Figure 2). The other major sources include cereals (419 entries), fish (384 entries), bovine (477 entries), pork/porcine (333 entries), chicken (177 entries), casein (723 entries), soybean (159 entries), egg (97 entries), human (215) and others (1152 entries). No source information was provided in case of 1805 entries hence marked as ‘ND’, i.e. Not Described. Some peptide entries occur in more than one class and are therefore overlapping. For example, an entry having source described as ‘Milk casein’ occurs in ‘Milk’ class as well as in ‘Casein’ class. In AHTPDB, almost all AHTPs target ‘angiotensin-I converting enzyme (ACE)’. Many such peptides have also been used as food additives. Therefore, toxicity/bitterness values of these peptides are of much importance and thus we have compiled these values (156 entries) in the database. Toxicity values may help in designing significant AHTPs with high efficacy but least toxicity or bitterness to be used as food additives. In AHTPDB, most of the peptides have been evaluated by two assays developed by Cushman & Cheung (35) and Kasahara & Ashihara (36). A total of 1182 and 218 entries have been made for these two assays, respectively. Most of the AHTPs have been identified and purified by using RP-HPLC, gel filteration chromatography (GFC), size exclusion chromatography (SEC), ion exchange chromatography (IEC), ultrafiltration (UF), thin layer chromatography (TLC), etc. A number of peptides have been tested on Spontaneously Hypertensive Rats (SHR) or Dahl Salt-Sensitive Rats (DSSR) in order to check the antihypertensive effect of peptides. In this study, we collected all the values (maximum decrease in SBP) wherever provided in the literature. Also, we approximated the value of decrease in SBP where exact value was not given but represented in the form of graphs.


AHTPDB: a comprehensive platform for analysis and presentation of antihypertensive peptides.

Kumar R, Chaudhary K, Sharma M, Nagpal G, Chauhan JS, Singh S, Gautam A, Raghava GP - Nucleic Acids Res. (2014)

Distribution of antihypertensive peptides in AHTPDB database based on various sources.
© Copyright Policy - creative-commons
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4383949&req=5

Figure 2: Distribution of antihypertensive peptides in AHTPDB database based on various sources.
Mentions: AHTPs have been isolated from various sources, including natural food, fungi, algae, microorganism, insects or snake venom. Among natural food sources, milk is the most explored source for identification of AHTPs with 834 entries (Figure 2). The other major sources include cereals (419 entries), fish (384 entries), bovine (477 entries), pork/porcine (333 entries), chicken (177 entries), casein (723 entries), soybean (159 entries), egg (97 entries), human (215) and others (1152 entries). No source information was provided in case of 1805 entries hence marked as ‘ND’, i.e. Not Described. Some peptide entries occur in more than one class and are therefore overlapping. For example, an entry having source described as ‘Milk casein’ occurs in ‘Milk’ class as well as in ‘Casein’ class. In AHTPDB, almost all AHTPs target ‘angiotensin-I converting enzyme (ACE)’. Many such peptides have also been used as food additives. Therefore, toxicity/bitterness values of these peptides are of much importance and thus we have compiled these values (156 entries) in the database. Toxicity values may help in designing significant AHTPs with high efficacy but least toxicity or bitterness to be used as food additives. In AHTPDB, most of the peptides have been evaluated by two assays developed by Cushman & Cheung (35) and Kasahara & Ashihara (36). A total of 1182 and 218 entries have been made for these two assays, respectively. Most of the AHTPs have been identified and purified by using RP-HPLC, gel filteration chromatography (GFC), size exclusion chromatography (SEC), ion exchange chromatography (IEC), ultrafiltration (UF), thin layer chromatography (TLC), etc. A number of peptides have been tested on Spontaneously Hypertensive Rats (SHR) or Dahl Salt-Sensitive Rats (DSSR) in order to check the antihypertensive effect of peptides. In this study, we collected all the values (maximum decrease in SBP) wherever provided in the literature. Also, we approximated the value of decrease in SBP where exact value was not given but represented in the form of graphs.

Bottom Line: In addition, the database provides structural information of these peptides that includes predicted tertiary and secondary structures.A user-friendly web interface with various tools has been developed to retrieve and analyse the data.It is anticipated that AHTPDB will be a useful and unique resource for the researchers working in the field of antihypertensive peptides.

View Article: PubMed Central - PubMed

Affiliation: Bioinformatics Centre, CSIR-Institute of Microbial Technology, Chandigarh 160036, India.

Show MeSH
Related in: MedlinePlus