Interaction of α-Lactalbumin with Mini-αA-Crystallin
αA-Crystallin can function like a molecular chaperone. We have recently shown that residues 71-88 in αA-crystallin represent the “chaperone active site” of the protein. A peptide containing the sequence of αA-crystallin sequence DFVIFLDVKHFSPEDLTVK (mini αA-crystallin) by itself displays the antiagg...
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| Veröffentlicht in: | Journal of Protein Chemistry 2001-02, Vol.20 (2), p.123-130 |
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| creator | Sreelakshmi, Y. Sharma, K. Krishna |
| description | αA-Crystallin can function like a molecular chaperone. We have recently shown that residues 71-88 in αA-crystallin represent the “chaperone active site” of the protein. A peptide containing the sequence of αA-crystallin sequence DFVIFLDVKHFSPEDLTVK (mini αA-crystallin) by itself displays the antiaggregation property of αA-crystallin. We have prepared a complex of reduced α-lactalbumin and mini-αA-crystallin and investigated the nature, conformation, and properties of the complex by dynamic light scattering, HPLC analysis, CD spectroscopy, and fluorescence studies. Although mini-αA was able to prevent the precipitation of reduced α-lactalbumin, large aggregates (50-500 nm) of the complex were formed during the assay. Amino acid composition estimation revealed that α-lactalbumin and mini-αA-crystallin were present in 1:2 ratio in the aggregates. During our study significant red shift in the Trp fluorescence emission maximum and an increase in Bis-ANS binding to the mini αA-crystallin-bound α-lacatalbumin were observed. The CD spectra of the complex showed a significant loss of α-helical content but the β-sheet content appeared to be less affected, indicating the molten-globule state of the reduced lactalbumin in the complex. These data show that the active site of αA-crystallin by itself can maintain a significantly denatured and unfolded protein in soluble form. |
| doi_str_mv | 10.1023/A:1011077307262 |
| format | Article |
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Krishna</creator><creatorcontrib>Sreelakshmi, Y. ; Sharma, K. Krishna</creatorcontrib><description>αA-Crystallin can function like a molecular chaperone. We have recently shown that residues 71-88 in αA-crystallin represent the “chaperone active site” of the protein. A peptide containing the sequence of αA-crystallin sequence DFVIFLDVKHFSPEDLTVK (mini αA-crystallin) by itself displays the antiaggregation property of αA-crystallin. We have prepared a complex of reduced α-lactalbumin and mini-αA-crystallin and investigated the nature, conformation, and properties of the complex by dynamic light scattering, HPLC analysis, CD spectroscopy, and fluorescence studies. Although mini-αA was able to prevent the precipitation of reduced α-lactalbumin, large aggregates (50-500 nm) of the complex were formed during the assay. Amino acid composition estimation revealed that α-lactalbumin and mini-αA-crystallin were present in 1:2 ratio in the aggregates. During our study significant red shift in the Trp fluorescence emission maximum and an increase in Bis-ANS binding to the mini αA-crystallin-bound α-lacatalbumin were observed. The CD spectra of the complex showed a significant loss of α-helical content but the β-sheet content appeared to be less affected, indicating the molten-globule state of the reduced lactalbumin in the complex. These data show that the active site of αA-crystallin by itself can maintain a significantly denatured and unfolded protein in soluble form.</description><identifier>ISSN: 0277-8033</identifier><identifier>ISSN: 1572-3887</identifier><identifier>EISSN: 1573-4943</identifier><identifier>DOI: 10.1023/A:1011077307262</identifier><language>eng</language><publisher>New York: Springer Nature B.V</publisher><subject>Aggregates ; Amino acid composition ; Amino acids ; Crystallin ; Doppler effect ; Emission analysis ; Fluorescence ; Lactalbumin ; Light scattering ; Liquid chromatography ; Molecular biology ; Peptides ; Photon correlation spectroscopy ; Protein folding ; Proteins ; Red shift ; Spectroscopy ; Spectrum analysis</subject><ispartof>Journal of Protein Chemistry, 2001-02, Vol.20 (2), p.123-130</ispartof><rights>Plenum Publishing Corporation 2001.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c336t-fb7813f795a5bc328d966d0b4c617ede1a5de39a1cba35a1c8ade533afd88123</citedby><cites>FETCH-LOGICAL-c336t-fb7813f795a5bc328d966d0b4c617ede1a5de39a1cba35a1c8ade533afd88123</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids></links><search><creatorcontrib>Sreelakshmi, Y.</creatorcontrib><creatorcontrib>Sharma, K. Krishna</creatorcontrib><title>Interaction of α-Lactalbumin with Mini-αA-Crystallin</title><title>Journal of Protein Chemistry</title><description>αA-Crystallin can function like a molecular chaperone. We have recently shown that residues 71-88 in αA-crystallin represent the “chaperone active site” of the protein. A peptide containing the sequence of αA-crystallin sequence DFVIFLDVKHFSPEDLTVK (mini αA-crystallin) by itself displays the antiaggregation property of αA-crystallin. We have prepared a complex of reduced α-lactalbumin and mini-αA-crystallin and investigated the nature, conformation, and properties of the complex by dynamic light scattering, HPLC analysis, CD spectroscopy, and fluorescence studies. Although mini-αA was able to prevent the precipitation of reduced α-lactalbumin, large aggregates (50-500 nm) of the complex were formed during the assay. Amino acid composition estimation revealed that α-lactalbumin and mini-αA-crystallin were present in 1:2 ratio in the aggregates. During our study significant red shift in the Trp fluorescence emission maximum and an increase in Bis-ANS binding to the mini αA-crystallin-bound α-lacatalbumin were observed. The CD spectra of the complex showed a significant loss of α-helical content but the β-sheet content appeared to be less affected, indicating the molten-globule state of the reduced lactalbumin in the complex. These data show that the active site of αA-crystallin by itself can maintain a significantly denatured and unfolded protein in soluble form.</description><subject>Aggregates</subject><subject>Amino acid composition</subject><subject>Amino acids</subject><subject>Crystallin</subject><subject>Doppler effect</subject><subject>Emission analysis</subject><subject>Fluorescence</subject><subject>Lactalbumin</subject><subject>Light scattering</subject><subject>Liquid chromatography</subject><subject>Molecular biology</subject><subject>Peptides</subject><subject>Photon correlation spectroscopy</subject><subject>Protein folding</subject><subject>Proteins</subject><subject>Red shift</subject><subject>Spectroscopy</subject><subject>Spectrum analysis</subject><issn>0277-8033</issn><issn>1572-3887</issn><issn>1573-4943</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2001</creationdate><recordtype>article</recordtype><sourceid>BENPR</sourceid><recordid>eNpVUM1Kw0AYXETBGD17Dd7Xfpsv-xNvoWgtRLz0vmySDW5Jk7qbIH2svkifyZR68TQMM8wwQ8gjg2cGKS6KFwaMgZQIMhXpFYkYl0izPMNrEkEqJVWAeEvuQtgCQK4URESs-9F6U49u6JOhTU5HWs7MdNW0c33y48av5MP1jp6OBV36Q5ilzvX35KY1XbAPfxiTzdvrZvlOy8_VelmUtEYUI20rqRi2MueGVzWmqsmFaKDKasGkbSwzvLGYG1ZXBvkMyjSWI5q2UYqlGJOnS-zeD9-TDaPeDpPv50adC-Qoz8tjsriYaj-E4G2r997tjD9oBvps0IX-dw3-Ak1KVtY</recordid><startdate>20010201</startdate><enddate>20010201</enddate><creator>Sreelakshmi, Y.</creator><creator>Sharma, K. 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Krishna</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Interaction of α-Lactalbumin with Mini-αA-Crystallin</atitle><jtitle>Journal of Protein Chemistry</jtitle><date>2001-02-01</date><risdate>2001</risdate><volume>20</volume><issue>2</issue><spage>123</spage><epage>130</epage><pages>123-130</pages><issn>0277-8033</issn><issn>1572-3887</issn><eissn>1573-4943</eissn><abstract>αA-Crystallin can function like a molecular chaperone. We have recently shown that residues 71-88 in αA-crystallin represent the “chaperone active site” of the protein. A peptide containing the sequence of αA-crystallin sequence DFVIFLDVKHFSPEDLTVK (mini αA-crystallin) by itself displays the antiaggregation property of αA-crystallin. We have prepared a complex of reduced α-lactalbumin and mini-αA-crystallin and investigated the nature, conformation, and properties of the complex by dynamic light scattering, HPLC analysis, CD spectroscopy, and fluorescence studies. Although mini-αA was able to prevent the precipitation of reduced α-lactalbumin, large aggregates (50-500 nm) of the complex were formed during the assay. Amino acid composition estimation revealed that α-lactalbumin and mini-αA-crystallin were present in 1:2 ratio in the aggregates. During our study significant red shift in the Trp fluorescence emission maximum and an increase in Bis-ANS binding to the mini αA-crystallin-bound α-lacatalbumin were observed. The CD spectra of the complex showed a significant loss of α-helical content but the β-sheet content appeared to be less affected, indicating the molten-globule state of the reduced lactalbumin in the complex. These data show that the active site of αA-crystallin by itself can maintain a significantly denatured and unfolded protein in soluble form.</abstract><cop>New York</cop><pub>Springer Nature B.V</pub><doi>10.1023/A:1011077307262</doi><tpages>8</tpages></addata></record> |
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| subjects | Aggregates Amino acid composition Amino acids Crystallin Doppler effect Emission analysis Fluorescence Lactalbumin Light scattering Liquid chromatography Molecular biology Peptides Photon correlation spectroscopy Protein folding Proteins Red shift Spectroscopy Spectrum analysis |
| title | Interaction of α-Lactalbumin with Mini-αA-Crystallin |
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