Antibacterial activity of active peptide from marine macroalgae Chondrus crispus protein hydrolysate against Staphylococcus aureus
Macroalgae is a protein source with the potential to yield antimicrobial peptides (AMPs) that exhibit a wide range of biological activities. This study aimed to find bioactive peptide-based antibacterial compounds from marine macroalgae Chondrus crispus protein hydrolysate. The peptides were isolate...
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| Veröffentlicht in: | Farmacija 2023-10, Vol.70 (4), p.983-992 |
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| container_title | Farmacija |
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| creator | Habibie, Ahmad Raharjo, Tri Joko Swasono, Respati Tri Retnaningrum, Endah |
| description | Macroalgae is a protein source with the potential to yield antimicrobial peptides (AMPs) that exhibit a wide range of biological activities. This study aimed to find bioactive peptide-based antibacterial compounds from marine macroalgae
Chondrus crispus
protein hydrolysate. The peptides were isolated by solid phase extraction with a strong cation exchanger from trypsin-digested and
α
-chymotrypsin-digested hydrolysates. Certain fractions of the hydrolyzed protein displayed a good inhibition zone, with the α-chymotrypsin-digested fraction eluted at pH 9 exhibiting the highest inhibition against Gram-negative bacteria
Staphylococcus aureus
. Several peptides were characterized as cationic helical peptides with hydrophobicity percentages of 16.67–77.78%. The potential antibacterial peptide P01 KKNVTTLAPLVF was identified as an
α
-helical cationic antibacterial peptide with 0.525 GRAVY value, amphipathic structure, and +2 total charge. Moreover, strong interaction was observed between P07 SAGSGNEGLSGW and P20 RTASSR peptide with DNA gyrase and DHFR receptors from
S. aureus
with binding energy -8.0 and -7.3 kcal/mol, respectively. |
| doi_str_mv | 10.3897/pharmacia.70.e112215 |
| format | Article |
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Chondrus crispus
protein hydrolysate. The peptides were isolated by solid phase extraction with a strong cation exchanger from trypsin-digested and
α
-chymotrypsin-digested hydrolysates. Certain fractions of the hydrolyzed protein displayed a good inhibition zone, with the α-chymotrypsin-digested fraction eluted at pH 9 exhibiting the highest inhibition against Gram-negative bacteria
Staphylococcus aureus
. Several peptides were characterized as cationic helical peptides with hydrophobicity percentages of 16.67–77.78%. The potential antibacterial peptide P01 KKNVTTLAPLVF was identified as an
α
-helical cationic antibacterial peptide with 0.525 GRAVY value, amphipathic structure, and +2 total charge. Moreover, strong interaction was observed between P07 SAGSGNEGLSGW and P20 RTASSR peptide with DNA gyrase and DHFR receptors from
S. aureus
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Chondrus crispus
protein hydrolysate. The peptides were isolated by solid phase extraction with a strong cation exchanger from trypsin-digested and
α
-chymotrypsin-digested hydrolysates. Certain fractions of the hydrolyzed protein displayed a good inhibition zone, with the α-chymotrypsin-digested fraction eluted at pH 9 exhibiting the highest inhibition against Gram-negative bacteria
Staphylococcus aureus
. Several peptides were characterized as cationic helical peptides with hydrophobicity percentages of 16.67–77.78%. The potential antibacterial peptide P01 KKNVTTLAPLVF was identified as an
α
-helical cationic antibacterial peptide with 0.525 GRAVY value, amphipathic structure, and +2 total charge. Moreover, strong interaction was observed between P07 SAGSGNEGLSGW and P20 RTASSR peptide with DNA gyrase and DHFR receptors from
S. aureus
with binding energy -8.0 and -7.3 kcal/mol, respectively.</description><subject>Bacteria</subject><subject>Drug resistance in microorganisms</subject><subject>Force and energy</subject><subject>Mass spectrometry</subject><subject>Methicillin</subject><subject>Peptides</subject><subject>Protein hydrolysates</subject><subject>Staphylococcus aureus</subject><issn>0428-0296</issn><issn>2603-557X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2023</creationdate><recordtype>article</recordtype><sourceid>DOA</sourceid><recordid>eNptUU1r3DAQNaWFLkn-QQ-Cnr2VZFuyjsvSj0Cgh7TQmxhJo10F2zKStuBrf3nVbggUyhze8HjzmJnXNO8Y3Xejkh_WM6QZbIC9pHtkjHM2vGp2XNCuHQb543Wzoz0fW8qVeNvc5fxEKeUjHRUfd82vw1KCAVswBZhIbcLPUDYS_bVHsuJagkPiU5zJDCksWMGmCNMJkBzPcXHpkolNIa8V1xQLhoWcN5fitGUoSOAEYcmFPBZYz9sUbbS2SuGS8JJvmzcepox3z3jTfP_08dvxS_vw9fP98fDQ2r6jpRXMqH700oiRm5EayYxxwhjaGzYMBsH4zknPBHYgFHfMU2WMlX5ENIMz3U1zf_V1EZ70mkI9ZtMRgv5LxHTSkEqwE2ovnOdMGEaHvrc9U50ZOhSqPhdB9kP1en_1OkGVh8XHksDOIVt9kFIoJfjIq2r_H1Uth3OwcUEfKv_PQH8dqO_NOaF_WZNR_Sdt_ZK2llQ_p939BouJo60</recordid><startdate>20231005</startdate><enddate>20231005</enddate><creator>Habibie, Ahmad</creator><creator>Raharjo, Tri Joko</creator><creator>Swasono, Respati Tri</creator><creator>Retnaningrum, Endah</creator><general>Pensoft Publishers</general><scope>AAYXX</scope><scope>CITATION</scope><scope>DOA</scope></search><sort><creationdate>20231005</creationdate><title>Antibacterial activity of active peptide from marine macroalgae Chondrus crispus protein hydrolysate against Staphylococcus aureus</title><author>Habibie, Ahmad ; Raharjo, Tri Joko ; Swasono, Respati Tri ; Retnaningrum, Endah</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c430t-61b948f7b682b80b71bbd6bb04b155beabf3d7f16e3a692d1f09bbc7f8eeb5db3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2023</creationdate><topic>Bacteria</topic><topic>Drug resistance in microorganisms</topic><topic>Force and energy</topic><topic>Mass spectrometry</topic><topic>Methicillin</topic><topic>Peptides</topic><topic>Protein hydrolysates</topic><topic>Staphylococcus aureus</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Habibie, Ahmad</creatorcontrib><creatorcontrib>Raharjo, Tri Joko</creatorcontrib><creatorcontrib>Swasono, Respati Tri</creatorcontrib><creatorcontrib>Retnaningrum, Endah</creatorcontrib><collection>CrossRef</collection><collection>DOAJ Directory of Open Access Journals</collection><jtitle>Farmacija</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Habibie, Ahmad</au><au>Raharjo, Tri Joko</au><au>Swasono, Respati Tri</au><au>Retnaningrum, Endah</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Antibacterial activity of active peptide from marine macroalgae Chondrus crispus protein hydrolysate against Staphylococcus aureus</atitle><jtitle>Farmacija</jtitle><date>2023-10-05</date><risdate>2023</risdate><volume>70</volume><issue>4</issue><spage>983</spage><epage>992</epage><pages>983-992</pages><issn>0428-0296</issn><eissn>2603-557X</eissn><abstract>Macroalgae is a protein source with the potential to yield antimicrobial peptides (AMPs) that exhibit a wide range of biological activities. This study aimed to find bioactive peptide-based antibacterial compounds from marine macroalgae
Chondrus crispus
protein hydrolysate. The peptides were isolated by solid phase extraction with a strong cation exchanger from trypsin-digested and
α
-chymotrypsin-digested hydrolysates. Certain fractions of the hydrolyzed protein displayed a good inhibition zone, with the α-chymotrypsin-digested fraction eluted at pH 9 exhibiting the highest inhibition against Gram-negative bacteria
Staphylococcus aureus
. Several peptides were characterized as cationic helical peptides with hydrophobicity percentages of 16.67–77.78%. The potential antibacterial peptide P01 KKNVTTLAPLVF was identified as an
α
-helical cationic antibacterial peptide with 0.525 GRAVY value, amphipathic structure, and +2 total charge. Moreover, strong interaction was observed between P07 SAGSGNEGLSGW and P20 RTASSR peptide with DNA gyrase and DHFR receptors from
S. aureus
with binding energy -8.0 and -7.3 kcal/mol, respectively.</abstract><pub>Pensoft Publishers</pub><doi>10.3897/pharmacia.70.e112215</doi><tpages>10</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Farmacija, 2023-10, Vol.70 (4), p.983-992 |
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| language | eng |
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| source | DOAJ Directory of Open Access Journals; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals |
| subjects | Bacteria Drug resistance in microorganisms Force and energy Mass spectrometry Methicillin Peptides Protein hydrolysates Staphylococcus aureus |
| title | Antibacterial activity of active peptide from marine macroalgae Chondrus crispus protein hydrolysate against Staphylococcus aureus |
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