Browse

This section provides multiple options to explore tumor homing peptides based on various criteria.

Major Fields

This interface enables users to browse the database by the following key fields:

  • Target Tumor
  • Cell Line
  • Year of Publication
  • Target Site
Major Fields

Amino Acid Frequency and Composition

Filter sequences by amino acid frequency and composition. For example, setting Lysine values between 3 and 23 will retrieve all sequences with Lysine counts in that range. You can combine this with other amino acid criteria (e.g., Glycine between 4 and 18) to further refine the results. This method also applies to filtering by amino acid composition as well as physical property frequency and composition.

Amino Acid Frequency Amino Acid Composition

Physicochemical Property Frequency and Composition

Retrieve tumor homing peptides based on the frequency of specific residue types. You can:

  • Filter by residue types such as positive charge, negative charge, or polar residues.
  • Adjust default minimum and maximum values to customize your search range.
  • Example: Set an aromatic property range between 2 and 8 to display all peptides within that range.
  • Combine multiple property criteria (e.g., aromatic property and positive charge) for more refined results.
Physicochemical Property Frequency

Physicochemical Property Values

Display tumor homing peptides that fall within user-defined ranges for the following properties:

  • Hydrophobicity
  • Hydrophilicity
  • Net Charge
  • Isoelectric Point
  • Molecular Weight

Enter the desired minimum and maximum values for each property to retrieve peptides that match your criteria.

Physicochemical Property Values

Structure

This section allows users to explore structural information of tumor homing peptides based on secondary structure and 3D models.

Secondary Structure Composition

Retrieve peptides based on the percentage composition of four different secondary structural states:

  • Helix (H)
  • Beta Sheet (E)
  • Turn (T)
  • Coil (C)

Define the minimum and maximum percentage values for each structural type to filter the results.

Secondary Structure Composition

3D Structures

Three-dimensional structures of all tumor homing peptides have been predicted using the PEPstr tool.

3D Structures

Tools

This section provides computational tools for analyzing and comparing peptide sequences against the Tumor Homing Peptide database.

BLAST 🔗

Perform a similarity-based search of a query sequence against the Tumor Homing Peptide database using BLAST.

  • Enter the query sequence using single-letter amino acid codes.
  • The tool returns all peptides from the database that show similarity to the query.
BLAST Tool

Smith-Waterman

This tool identifies regions of local similarity between the query peptide and peptides in the database.

  • Performs pairwise alignments by comparing all possible segments.
  • Optimizes similarity scores to provide precise alignment results.
Smith Waterman Tool

Identical Residues

Compares the query sequence with each peptide in the database to determine exact residue matches.

  • The sequence is aligned step-by-step with all database peptides.
  • The tool returns the count of identical residues for each pair.
Identical Residues Tool

Peptide Mapping

Slide the query peptide across all database sequences to find the best alignment with the highest number of identical residues.

Identical Residues Tool

Physical Properties

Calculate physical properties of a given peptide, including:

  • Hydrophobicity
  • Hydrophilicity
  • Net Charge
  • Isoelectric Point
  • Molecular Weight
Identical Residues Tool

Description of Fields

This table summarizes the various fields included in the Tumor Homing Peptide database along with their descriptions and examples.

Field Name Description Example
ID Unique identifier assigned to each tumor homing peptide in the database. 1025
REFERENCE Research article reference including author(s), journal, year, volume, and page numbers. He X et al. Mol Pharm. 2011 Apr 4;8(2):430-8.
SOURCE/ORIGIN Source from which the peptide was derived. Phage Display
MOTIF Specific sequence motif identified in the peptide. NGR
TARGET TUMOR Target tumor against which the peptide was developed. Lung
TARGET CELL Targeted cell type for the peptide. Endothelial cell
RECEPTOR Receptor that the peptide binds to or interacts with. Aminopeptidase N
END MODIFICATION Modifications made to the peptide termini (N-/C- terminus). FITC labeling at N-terminus & amidation at C-terminus
In vitro/ ex vivo Cell lines used for in vitro or ex vivo experiments. MDA-MB-231
In vivo Animal models used for in vivo studies. BALB C mice
PAYLOADS Conjugates attached to peptides for imaging or drug delivery. Doxorubicin
STRUCTURE Predicted 3D structure of peptides using Pepstr (only natural amino acids). 3D structure
NET CHARGE Net charge of the peptide. +1
HYDROPHOBICITY Overall hydrophobicity score of the peptide. 33.33
MOLECULAR WEIGHT Molecular weight of the peptide. 1025.32
pI Isoelectric point of the peptide. 4
AA FREQUENCY Count of each amino acid present in the peptide sequence. 5
AA COMPOSITION Percentage composition of each amino acid in the peptide. 50.00
SECONDARY STRUCTURE INFORMATION Secondary structural states (e.g., Helix, Coil, Strand) for each residue. Helix, Coil, Strand

Description of Cell Lines

This table provides detailed information about the cell lines used in the Tumor Homing Peptide Database, including their source, morphology, and growth characteristics.

Cell Line ATCC No. Organism Disease Source Organism Morphology Growth Properties
MDA-MB-231 HTB-26 Homo Sapiens Adenocarcinoma Mammary Gland Epithelial Adherent
MDA-MB-361 HTB-27 Homo Sapiens Adenocarcinoma Mammary Gland Epithelial Loosely Adherent
MDA-MB-435 HTB-129 Homo Sapiens Ductal Carcinoma Mammary Gland Spindal Adherent
MCF-7 HTB-22 Homo Sapiens Adenocarcinoma Mammary Gland Epithelial Adherent
SK-BR-3 HTB-30 Homo Sapiens Adenocarcinoma Mammary Gland Epithelial Adherent
HT-29 HTB-38 Homo Sapiens Colorectal Adenocarcinoma Colon Epithelial Adherent
BT-474 HTB-20 Homo Sapiens Ductal Carcinoma Mammary Gland Epithelial Adherent, patchy
BT-483 HTB-121 Homo Sapiens Ductal Carcinoma Mammary Gland Epithelial Adherent
HeLa CCL-2 Homo Sapiens Adenocarcinoma Cervix Epithelial Adherent
Ca Ski CRL-1550 Homo Sapiens Epidermoid Carcinoma Cervix Epithelial Adherent
A549 CCL-185 Homo Sapiens Carcinoma Lung Epithelial Adherent
A375 CRL-1619 Homo Sapiens Malignant Melanoma Skin Epithelial Adherent
PC-3 CRL-1435 Homo Sapiens Adenocarcinoma Ovary Epithelial Adherent
MDA-PCa-2b CRL-2422 Homo Sapiens Adenocarcinoma Prostate Epithelial Adherent
LNCaP CRL-1740 Homo Sapiens Carcinoma Prostate Epithelial Adherent
OVCAR-3 HTB-161 Homo Sapiens Adenocarcinoma Ovary Epithelial Adherent
H226 5826 Homo Sapiens Squamous Cell Carcinoma Lung Epithelial Adherent
H460 HTB-177 Homo Sapiens Large Cell Lung Cancer Lung Epithelial Adherent
ZR-75-1 CRL-1500 Homo Sapiens Ductal Carcinoma Mammary Gland Epithelial Adherent
Hep G2 HB-8065 Homo Sapiens Hepatocellular Carcinoma Liver Epithelial Adherent
MIA PaCa-2 CRL-1420 Homo Sapiens Carcinoma Pancreas Attached epithelial with floating rounded cells Adherent

Frequently Asked Questions (FAQs)

Q1. What is TumorHoPe?
TumorHoPe is a literature-based database of tumor homing peptides.

Q2. Why tumor homing /targeting peptides?
The biggest challenge of cancer chemotherapy is the lack of specificity and selectivity for the target. Peptide-based therapy such as tumor homing peptides are highly specific for their target. These peptides target either tumor cells or the microenvironment around them like blood vessels and lymph vessels.

Q3. How to search into TumorHoPe?
Users can search a peptide by name, peptide sequence, target tumor, cell lines, and PMID.

Q4. What other information one can get regarding peptide sequence?
The database provides amino acid composition, frequency, physicochemical properties like hydrophobicity and net charge, as well as secondary and tertiary structure information.

Q5. Is this database useful if users have their own query sequence?
Yes, users can use tools like BLAST, SMITH-WATERMAN, and peptide mapping. They can also obtain amino acid composition, frequency, and physicochemical properties.

Q6. Are all peptides used in the database experimentally validated?
Most peptides are obtained by using phage display, which yields clones for a particular target cell. The database provides details for clones with the highest recovery frequency.

Q7. Is tumor homing peptide a reality?
Yes, drugs are being conjugated with these peptides and are in different stages of clinical trials. For example, tTF-NGR peptide was used to treat a woman suffering from metastatic adenocarcinoma after four lines of chemotherapy.

Q8. Are there any peptides with modification?
Yes, some peptides contain modified amino acids. 'X' represents norleucine (an isomer of leucine); 'F*' represents 4-chlorophenylalanine; and lowercase letters indicate D-amino acids.
Note: In the case of bioconjugate peptides (tumor killing + homing peptide), only the homing peptide sequence is included in the database.