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autogel lanreotide  (Aladin Enterprises Inc)
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ipsen sa markets lanreotide  (Ipsen Group)
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somatuline  (Ipsen Group)
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On the top is the sequence of the native somatostatin peptide. The blue sequence in somatostatin represents a key pharmacophore in somatostatin, responsible for receptor binding. In somatostatin analogues, lysine (K) is conserved, while tryptophan is replaced with its stereoisomers in octreotide, <t>lanreotide,</t> vapreotide, and pasireotide. Phenylalanine is substituted with tyrosine, which has an additional hydroxyl group, and threonine is replaced with a more hydrophobic amino acid, such as valine, in lanreotide and vapreotide. Pasireotide incorporates the highest number of unnatural amino acids. In this analogue, cyclization occurs between the N- and C-terminal ends, while in octreotide, lanreotide, and vapreotide, cyclization involves the side chains of cysteine residues, similar to native somatostatin.
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somatuline depot  (Ipsen Group)
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On the top is the sequence of the native somatostatin peptide. The blue sequence in somatostatin represents a key pharmacophore in somatostatin, responsible for receptor binding. In somatostatin analogues, lysine (K) is conserved, while tryptophan is replaced with its stereoisomers in octreotide, <t>lanreotide,</t> vapreotide, and pasireotide. Phenylalanine is substituted with tyrosine, which has an additional hydroxyl group, and threonine is replaced with a more hydrophobic amino acid, such as valine, in lanreotide and vapreotide. Pasireotide incorporates the highest number of unnatural amino acids. In this analogue, cyclization occurs between the N- and C-terminal ends, while in octreotide, lanreotide, and vapreotide, cyclization involves the side chains of cysteine residues, similar to native somatostatin.
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somatuline depot - by Bioz Stars, 2026-08
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lanreotide  (Toronto Research Chemicals)
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Toronto Research Chemicals lanreotide
On the top is the sequence of the native somatostatin peptide. The blue sequence in somatostatin represents a key pharmacophore in somatostatin, responsible for receptor binding. In somatostatin analogues, lysine (K) is conserved, while tryptophan is replaced with its stereoisomers in octreotide, <t>lanreotide,</t> vapreotide, and pasireotide. Phenylalanine is substituted with tyrosine, which has an additional hydroxyl group, and threonine is replaced with a more hydrophobic amino acid, such as valine, in lanreotide and vapreotide. Pasireotide incorporates the highest number of unnatural amino acids. In this analogue, cyclization occurs between the N- and C-terminal ends, while in octreotide, lanreotide, and vapreotide, cyclization involves the side chains of cysteine residues, similar to native somatostatin.
Lanreotide, supplied by Toronto Research Chemicals, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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lanreotide - by Bioz Stars, 2026-08
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octreotide lar/lanreotide autogel  (Schmid GmbH)
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On the top is the sequence of the native somatostatin peptide. The blue sequence in somatostatin represents a key pharmacophore in somatostatin, responsible for receptor binding. In somatostatin analogues, lysine (K) is conserved, while tryptophan is replaced with its stereoisomers in octreotide, <t>lanreotide,</t> vapreotide, and pasireotide. Phenylalanine is substituted with tyrosine, which has an additional hydroxyl group, and threonine is replaced with a more hydrophobic amino acid, such as valine, in lanreotide and vapreotide. Pasireotide incorporates the highest number of unnatural amino acids. In this analogue, cyclization occurs between the N- and C-terminal ends, while in octreotide, lanreotide, and vapreotide, cyclization involves the side chains of cysteine residues, similar to native somatostatin.
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octreotide lar/lanreotide autogel - by Bioz Stars, 2026-08
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lanreotide  (Novartis)
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Novartis lanreotide
On the top is the sequence of the native somatostatin peptide. The blue sequence in somatostatin represents a key pharmacophore in somatostatin, responsible for receptor binding. In somatostatin analogues, lysine (K) is conserved, while tryptophan is replaced with its stereoisomers in octreotide, <t>lanreotide,</t> vapreotide, and pasireotide. Phenylalanine is substituted with tyrosine, which has an additional hydroxyl group, and threonine is replaced with a more hydrophobic amino acid, such as valine, in lanreotide and vapreotide. Pasireotide incorporates the highest number of unnatural amino acids. In this analogue, cyclization occurs between the N- and C-terminal ends, while in octreotide, lanreotide, and vapreotide, cyclization involves the side chains of cysteine residues, similar to native somatostatin.
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On the top is the sequence of the native somatostatin peptide. The blue sequence in somatostatin represents a key pharmacophore in somatostatin, responsible for receptor binding. In somatostatin analogues, lysine (K) is conserved, while tryptophan is replaced with its stereoisomers in octreotide, lanreotide, vapreotide, and pasireotide. Phenylalanine is substituted with tyrosine, which has an additional hydroxyl group, and threonine is replaced with a more hydrophobic amino acid, such as valine, in lanreotide and vapreotide. Pasireotide incorporates the highest number of unnatural amino acids. In this analogue, cyclization occurs between the N- and C-terminal ends, while in octreotide, lanreotide, and vapreotide, cyclization involves the side chains of cysteine residues, similar to native somatostatin.

Journal: Chemical Reviews

Article Title: Advances in Peptidomimetics for Next-Generation Therapeutics: Strategies, Modifications, and Applications

doi: 10.1021/acs.chemrev.4c00989

Figure Lengend Snippet: On the top is the sequence of the native somatostatin peptide. The blue sequence in somatostatin represents a key pharmacophore in somatostatin, responsible for receptor binding. In somatostatin analogues, lysine (K) is conserved, while tryptophan is replaced with its stereoisomers in octreotide, lanreotide, vapreotide, and pasireotide. Phenylalanine is substituted with tyrosine, which has an additional hydroxyl group, and threonine is replaced with a more hydrophobic amino acid, such as valine, in lanreotide and vapreotide. Pasireotide incorporates the highest number of unnatural amino acids. In this analogue, cyclization occurs between the N- and C-terminal ends, while in octreotide, lanreotide, and vapreotide, cyclization involves the side chains of cysteine residues, similar to native somatostatin.

Article Snippet: lanreotide , Somatuline , somatostatin analogue (SSA) , 2007 , Ipsen, Globopharm, Tercica , acromegaly, neuroendocrine tumors, and conditions with excess hormone secretion , SC.

Techniques: Sequencing, Binding Assay, Analogues

On the top is the sequence of the native somatostatin peptide. The blue sequence in somatostatin represents a key pharmacophore in somatostatin, responsible for receptor binding. In somatostatin analogues, lysine (K) is conserved, while tryptophan is replaced with its stereoisomers in octreotide, lanreotide, vapreotide, and pasireotide. Phenylalanine is substituted with tyrosine, which has an additional hydroxyl group, and threonine is replaced with a more hydrophobic amino acid, such as valine, in lanreotide and vapreotide. Pasireotide incorporates the highest number of unnatural amino acids. In this analogue, cyclization occurs between the N- and C-terminal ends, while in octreotide, lanreotide, and vapreotide, cyclization involves the side chains of cysteine residues, similar to native somatostatin.

Journal: Chemical Reviews

Article Title: Advances in Peptidomimetics for Next-Generation Therapeutics: Strategies, Modifications, and Applications

doi: 10.1021/acs.chemrev.4c00989

Figure Lengend Snippet: On the top is the sequence of the native somatostatin peptide. The blue sequence in somatostatin represents a key pharmacophore in somatostatin, responsible for receptor binding. In somatostatin analogues, lysine (K) is conserved, while tryptophan is replaced with its stereoisomers in octreotide, lanreotide, vapreotide, and pasireotide. Phenylalanine is substituted with tyrosine, which has an additional hydroxyl group, and threonine is replaced with a more hydrophobic amino acid, such as valine, in lanreotide and vapreotide. Pasireotide incorporates the highest number of unnatural amino acids. In this analogue, cyclization occurs between the N- and C-terminal ends, while in octreotide, lanreotide, and vapreotide, cyclization involves the side chains of cysteine residues, similar to native somatostatin.

Article Snippet: lanreotide , Somatuline depot , somatostatin analogue (SSA) , 2007 , Ipsen , acromegaly, neuroendocrine tumors, and conditions with excess hormone secretion , SC.

Techniques: Sequencing, Binding Assay, Analogues